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US20120177610A1 - Manufacturing and Purification Processes of Complex Protein found in Fraction IV to make a separated Apo, Transferrin , and Alpha 1 Anti strepsin (A1AT) or A combined Transferrin / Apo/Human Albumin/A1AT and all new found proteins - Google Patents

Manufacturing and Purification Processes of Complex Protein found in Fraction IV to make a separated Apo, Transferrin , and Alpha 1 Anti strepsin (A1AT) or A combined Transferrin / Apo/Human Albumin/A1AT and all new found proteins Download PDF

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US20120177610A1
US20120177610A1 US13/114,951 US201113114951A US2012177610A1 US 20120177610 A1 US20120177610 A1 US 20120177610A1 US 201113114951 A US201113114951 A US 201113114951A US 2012177610 A1 US2012177610 A1 US 2012177610A1
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Kieu Hoang
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Priority claimed from PCT/US2007/020258 external-priority patent/WO2008088403A2/fr
Priority claimed from US12/457,796 external-priority patent/US8013122B2/en
Priority claimed from US13/108,970 external-priority patent/US20120195953A1/en
Priority to US13/114,951 priority Critical patent/US20120177610A1/en
Application filed by Individual filed Critical Individual
Priority to PCT/US2011/038595 priority patent/WO2012121740A1/fr
Priority to PCT/US2011/038679 priority patent/WO2012121742A1/fr
Priority to TW101107169A priority patent/TW201309719A/zh
Priority to TW104101523A priority patent/TWI610938B/zh
Priority to TW101107176A priority patent/TWI508972B/zh
Priority to TW104101525A priority patent/TWI600661B/zh
Publication of US20120177610A1 publication Critical patent/US20120177610A1/en
Priority to US14/056,363 priority patent/US9649366B2/en
Priority to US14/056,410 priority patent/US20140140987A1/en
Abandoned legal-status Critical Current

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    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/55—Protease inhibitors
    • A61K38/57—Protease inhibitors from animals; from humans
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/36—Blood coagulation or fibrinolysis factors
    • A61K38/363—Fibrinogen
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/36—Blood coagulation or fibrinolysis factors
    • A61K38/37—Factors VIII
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/38—Albumins
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/39—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin, cold insoluble globulin [CIG]
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/40—Transferrins, e.g. lactoferrins, ovotransferrins
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/43—Enzymes; Proenzymes; Derivatives thereof
    • A61K38/46—Hydrolases (3)
    • A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
    • A61K38/482—Serine endopeptidases (3.4.21)
    • A61K38/4833—Thrombin (3.4.21.5)
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/43—Enzymes; Proenzymes; Derivatives thereof
    • A61K38/46—Hydrolases (3)
    • A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
    • A61K38/482—Serine endopeptidases (3.4.21)
    • A61K38/4866—Protein C (3.4.21.69)
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P17/00—Drugs for dermatological disorders
    • A61P17/14—Drugs for dermatological disorders for baldness or alopecia
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P21/00—Drugs for disorders of the muscular or neuromuscular system
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
    • A61P31/04—Antibacterial agents
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
    • A61P31/12—Antivirals
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P35/00—Antineoplastic agents
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/775—Apolipopeptides

Definitions

  • AIDS related cancers anal cancer, appendix cancer, bile duct, bladder, osteosarcoma, brain, breast, cervical, colon, esophagus, eye, gall bladder, gastric, other gastrointestinal, Intestines, head neck, heart, liver, hypopharyngeal, kidney, laryngeal, lip oral cavity, lung, mouth, nasal Parasal, ovarian, pancreas, parathyroid, penile, prostate, rectal, renal cell carcinoma, salivary, skin, Spleen, throat, testicular, urethral, Vaginal.
  • Leukemia's (Acute myeloid leukemia (M0-M7), lymphoma, marrow malignancy, acute lymphoid leukemia (Small, middle, large) MDS, Myeloid dysfunction syndrome and Anemia.
  • Mankind have been suffering for hundreds of years for all kind of diseases, cancers, Alzheimer, diabetic, Parkinson, Autism and specially the agonies that we have to go through with AIDS, HEPATITIS B, and HEPATITIS C and new kinds of Virus infections and epidemic Incidence which feared and affected the economy of the world like SARS in China, Taiwan, Hong Kong, Vietnam, Singapore, Canada in 2003, with outbreak of bird flu (H1 N5) 2004 in Europe, Vietnam, Thailand and most recently in 2010 in Mexico with the outbreak of (H1 N1) which caused the country to shut down for weeks and badly affected its economy.
  • AFODRAAS 1-85 contains various combinations of apolipoproteins ApoA1, ApoA2, ApoA4, Apo-B48, ApoB100, ApoCI, ApoCII, ApoCIII, Apo-D, Apo-E, Apo-H, and Apo(a), all of which contain Good Healthy cells, as well as Alpha 1 Antitrypsin (A1AT), which is known also to contain Good Healthy Cells, Transferrin, which contains Good Healthy Cells, and Human Albumin, another Good Healthy cell Protein, together with a group of at least 20 unidentified discovered proteins which are being identified and characterized with the assistance of Academy of Science of China, the group containing Good Healthy cells.
  • A1AT Alpha 1 Antitrypsin
  • AFCC 1-85 (also referred to herein as “AFCCRAAS 1-85”, “AFCCRAAS 1”, “AFCCRAAS” and “AFCC”) contains various combinations of Prothrombin Complex Concentrate including all 13 Factors found in Fraction III, Alpha 1 Antitrypsin (A1AT), Transferrin, Human Albumin, and Anti thrombin III, all of which contain Good healthy cell proteins.
  • the combinations of AFCC 1-85 can also contain Transferrin, which contains Good Healthy Cells, and Human Albumin, another Good Healthy cell Protein, together with a group of at least 20 unidentified discovered proteins which are being identified and characterized with the assistance of Academy of Science of China, the group containing Good Healthy cells. Each combination will be applied to a certain number of diseases, including solid and Blood cancers.
  • the definition of death belongs to the beating of the heart, but if the LIVER will not manufacture, moderate, regulate and distribute Good Blood cells to the heart, the heart will not function.
  • the LIVER has become the most important ORGAN of the body as the liver Produce Antibodies and Proteins which are used to cure diseases and viruses as well as bacteria infection.
  • the liver is the largest organ in the body weighting approximately 1.4 kg. It is located on the right side of belly. Right under the chest bone. It has two pieces. The right piece is larger and consists of 3 smaller pieces together. The left piece is smaller, right on top of stomach adjacent to the throat.
  • the structure of the liver consists of from 50,000 to 100,000 small pieces with portal Vein in the middle. From the portal vein, hundreds of liver cells mix with pile system and very tiny blood vessels. With approximately 300 billion of cells (Approximately 30% of a trillion of cells in our body.
  • liver It has the ability to restore and maintain its function in case for any reason it has lost 90% of the liver. None of other Organ which has only 10% can function in our body. If 100% of the liver has been damaged due to the diseases a person can only live with a piece of Liver transplant. The liver receives blood through portal vein and Arterial vein. Every minute all these blood vessel has transferred to liver approximately 1.5 liter of blood. Blood in Arterial vein contain plenty of oxygen as for Blood in portal vein transport all waste from digestion. Liver is considered as a sophisticated chemical manufacturer/moderator/regulator/distributor with hundreds of Different important tasks:
  • Liver is the warehouse to receive glucose from small intestine store as Glycogen. After each meal, when the blood pressure increases, insulin from pancreas will help the liver to transform Glucose into glycogen. In a few hours later when the blood pressure decreases, the liver again to transform Glycogen into glucose then send Glucose to the blood then distribute to other organs or components which need Glucose. Diabetic people cannot receive insulin produced by pancreas due to the accumulation of Glucose from foods in the liver. 2. Beside the above task, liver also transform glucose and fat into protein and it also transform protein and fat into glucose. 3. The liver produces approximately 0.5-0.9 liter of pile every day. Pile is a liquid with the YELLOW-BLUE color,
  • Liver can eliminate some toxicity like alcohol and a few drugs like acetaminophen. 5. The liver produces urea, a waste from the protein and eliminate through kidney. 6. THE LIVER DESTROY ALL DAMAGED OR OLD RED CELLS as well DESTROY ALL BACTERIA in the Foods in the intestine. 7. The Liver contains Vitamins, A, B, D, E and K 8. Liver creates the protein in the blood like Albumin, Globulin and Coagulation.
  • FAT is a creative element of CELLS. Whenever FAT in the liver exceeds around 5% of the liver, attack and occupy All healthy cells then there will be a problem. At this time, Liver will have a Fatty Yellow color, the liver becomes bigger and heavier than its normalcy.
  • Tissue factor cells surrounding blood vessels will take away TOXICITY, BACTERIA, FAT to Transform Blood into CLEANER. Liver is like a filter. If now in liver cells and the space between the liver cells, are full of FAT
  • MACROPHAGE in Greek language BIG EATERS from makros “Large”+Phagein (EAT) are WHITE BLOOD CELLS produced by the differentiation of Monocytes in tissues. Human macrophages are about 21 micrometers in diameter. Monocytes and Marcophages are phacocytes. Macrophages function in both NON SPECIFIC DEFENSE (innate immunity) as well as initiate DENFENSE MECHANISIMS (Adaptive Immunity). Their role is to PHAGOCYTOSE (ENGULF and then DIGEST) cellular debris and pathogens.
  • NON SPECIFIC DEFENSE innate immunity
  • DENFENSE MECHANISIMS Adaptive Immunity
  • MARCHOPHAGE are IMPORTANT and GOOD HEALTHY CELLS Play a VERY IMPORTANT ROLE in the BODY's DEFENSE SYSTEM such as LIVER by ENGULF and then DIGEST Bacteria and other foreign particles.
  • Complement in the liver is a group of protein that play a part in the IMMUNE SYSTEM's DEFENSES against INFECTION.
  • Marcophages Due to their role in phagocytosis, Marcophages are involved in many diseases of the IMMUNE SYSTEM. Like HIV infection, Marcophages play a role in Human Immunodeficiency Virus (HIV) infection. Like T cells, macrophages can be infected with HIV, and even become a reservoir of on going virus replication throughout the body. Due to the LACK of GOOD HEALTHY CELLS in the body; the BAD INFECTED CELLS has gone through the System in the LIVER and The BAD CELLS EAT THE BAD CELLS AGAIN That is why VIRUS REPLICATE. Our Study NAT Testing of a POSITIVE by NAT of HIV 1,2 has shown the reduction of IU/ML after three days of introducing our AFODRAAS 1 and AFCCRAAS 1 into the HIV 1,2 POSITIVE PLASMA.
  • HIV Human Immunodeficiency Virus
  • HEART DISEASE Marcophages are the predominant cells involved in creating the PROGRESSIVE PLAQUE LESIONS of ARTHEROSCLEROSIS. That is why lowering down Triglycerides, VLDL, LDL, and increasing HDL WILL NOT REMOVE THE PLAQUE LESIONS by a FOREIGN SUBSTANCES like CHEMICALS that DO NOT CONTAIN a GOOD HEALTHY MARCOPHAGE CELL or Some other GOOD HEALTHY CELLS which have not been discovered as We have seen a lot more of proteins found in Fraction III of plasma under investigation. In our study of 52 Rabbits has proven this.
  • TUBERCULOSIS Once engulfed by a macrophage the causative agent of tuberculosis, Mycobacterium tuberculosis avoids cellular defenses and uses the cell to replicate.
  • Macrophages are believed to help cancer cells proliferate as well. They are attracted to oxygen-starved (hypoxic) tumor cells and promote chronic inflammation. Inflammatory compounds such Tumor necrosis factor (TNF) released by the macrophage activates the gene switch nuclear factor -kappa B.NF-kB then enters the nucleus of a tumor cell and turns on production of PROTEINS that stop apoptosis and promote cell proliferation and inflammation.
  • TNF Tumor necrosis factor
  • any of the single protein or combined protein of the above that contains any of one of good cells namely Neutrophil, Lymphocyte, Eosinophil, Basophil and MARCOPHAGE and it is possible That new cells may be found as we have found a lot more of Protein in the Fraction III of plasma under investigation.
  • Urine has been used to make UROKINASE for the treatment of stroke.
  • Urea fertilizer has been used for years in order to kill all worms, insecticides, buds in the soil to fertilize the soil for growing rice, vegetables, fruits.
  • HBV Hepatitis B Virus
  • HIV Human Immunodeficiency virus in 1983
  • HCV Hepatitis C Antibody virus
  • CJD Creutzfeldt-Jakob Disease prion
  • v-CJD Variant Creutzfeldt-Jakob disease prion
  • SARS-CoV severe Acute Respiratory Syndrome corona virus 2004, West Nile Virus (WNV) in 2005
  • WNV West Nile Virus
  • H1N5 Bird Flu virus
  • HCV Hepatitis C Virus
  • Hepatitis A a non enveloped virus which cannot be killed by Solvent Detergent method Contaminated in Factor VIII in many countries in Europe.
  • AFODRAAS 1 and AFCC RAAS1 have killed some kind of lethal Bacteria like Staphylococcus aureus that are resistant to our current antibiotic arsenal MARSA (Methicillin-Resistant Staphylococcus aureus which currently kill approximately 20,000 people a year in the US according to Forbes Feb. 14, 2011. Potential indications for all bacteria and SEPSIS which kill about 200,000 people a year in US out of 700,000 people having SEPSIS with LARGE dosages.
  • MARSA Metal-Resistant Staphylococcus aureus which currently kill approximately 20,000 people a year in the US according to Forbes Feb. 14, 2011.
  • Potential indications for all bacteria and SEPSIS which kill about 200,000 people a year in US out of 700,000 people having SEPSIS with LARGE dosages.
  • Hemophiliac A, B and VwB One of the liver function is to produce Coagulant, however these Hemophiliac lack Good HEALTHY Cells for the liver to produce Coagulant.
  • the liver is the ONLY ORGAN which produces PROTEINS and ANTIBODIES, both of which play a very important roles in the defense of people against diseases, viruses, bacteria infections.
  • This discovery reveals any protein that contains A GOOD HEALTHY CELL will properly can be used against Any diseases, viruses, bacteria, deficiencies, inhibitors, prion in our body and thus from now on civilization will be protected Against all kinds of diseases, cancers, epidemics, viruses, bacteria and possibly blind, deaf, mute people may benefit.
  • the Cells of the blood can be divided into: white blood cells, red blood cells and platelets.
  • Red blood cells or erythrocytes are the most common type of blood cell and our principal means of delivering oxygen to the body tissues through the circulatory system (arteries). Red blood cells take up oxygen in the lungs and release it while circulating through the body's capillary vessels (the smallest structures that conduct blood), where they take up carbon dioxide, which is a waste product of metabolism, and take it to the lungs, to be discarded through the respiration. These cells are rich in hemoglobin, which is a molecule that contains iron and that can bind oxygen (and is responsible for the blood's red color).
  • the red blood cells develop in the bone marrow and circulate for about 100-120 days in the body before their components are recycled by macrophages.
  • Red blood cells do not participate in the immune system.
  • Platelets are cell fragments (that is, cells that do not have a nucleus, 2-3 ⁇ m in diameter, which are derived from fragmentation of precursor cells known as “megakaryocytes”.
  • the average lifespan of a platelet is normally just 5 to 9 days. Platelets play a fundamental role in hemostasis with the formation of clots, but they do not participate in the immune system.
  • White blood cells are cells of the immune system involved in defending the body against both infectious disease and foreign materials.
  • leucocytes There are five different and diverse types of leukocytes exist, but they are all produced and derived from a multi potent cell in the bone marrow, known as a hematopoietic stem cell.
  • Leukocytes are found throughout the body, not only in the blood and the lymphatic system.
  • the number of white blood cells in the blood is often an indicator of disease. There are normally between 5′000 to 10′000 white blood cells per mL. An increase in the number of leukocytes over the upper limits s called leukocytosis, and a decrease below the lower limit is called leukopenia.
  • Type of cell % Main targets Lifetime Neutrophil 54-62 Bacteria and fungi 6 hs to a few days Lymphocyte 25-33 B Lymphocytes (releases antibodies and Weeks to assist “activation” of T lymphocytes) years
  • Cytotoxic T lymphocytes CD8+ virus- infected and tumor cells
  • Gamma-delta T lymphocytes shocks the functioning of the immune system back to normal operation after infection and prevents autoimmunity Natural killer T lymphocytes (virus- infected and tumor cells)
  • Eosinophil 1-6 Larger parasites 8-12 days Modulate allergic inflammatory responses Basophil ⁇ 1 Release mediators (histamine) in Hours to inflammatory response days Monocyte 2-10 Monocytes migrate from the blood- Hours to stream to other tissues and differ- days entiate into tissue resident macro- phages or dendritic cells Macrophage No* Phagocytos
  • Chylomicrons Mainnly Triglycerides which is considered very BAD according to a lot of publications and it may lead to Heart attack and Stroke.
  • FATS and cholesterol cannot Move within the water-based solution of the Blood stream.
  • Chylomicrons are large lipoprotein particles that consist of triglycerides (85-92%), phospholipids (6-12%), cholesterol (1-3%) and proteins (1-2%) [1]. They transport dietary lipids from the intestines to other locations in the body. Chylomicrons are one of the five major groups of lipoproteins (chylomicrons, VLDL, IDL, LDL, HDL) that enable fats and cholesterol to move within the water-based solution of the bloodstream.
  • Chylomicrons transport exogenous lipids to liver, adipose, cardiac, and skeletal muscle tissue, where their triglyceride components are unloaded by the activity of lipoprotein lipase. As a consequence, chylomicron remnants are left over and are taken up by the liver.
  • Chylomicrons are a type of lipoprotein produced in absorptive cells of small intestines, specifically, the epithelial cells within the villi of the duodenum.
  • Chylomicrons are created by the absorptive cells of the small intestine, known as enterocytes. They are relatively large, having a diameter of 75 to 1,200 nm. These nascent chylomicrons are released by exocytosis from enterocytes into lacteals, lymphatic vessels originating in the villi of the small intestine, and are then secreted into the bloodstream at the thoracic duct's connection with the left subclavian vein.
  • Nascent chylomicrons are primarily composed of triglycerides (85%) and contain some cholesterol and cholesteryl esters.
  • the main apolipoprotein component is apolipoprotein B-48 (APOB48).
  • chylomicrons While circulating in lymph and blood, chylomicrons exchange components with high-density lipoproteins (HDL).
  • HDL donates apolipoprotein C-II (APOC2) and lipoprotein E (APOE) to the nascent chylomicron and thus converts it to a mature chylomicron (often referred to simply as “chylomicron”).
  • APOC2 is the cofactor for lipoprotein lipase (LPL) activity.
  • the chylomicron returns APOC2 to the HDL (but keeps APOE), and, thus, becomes a chylomicron remnant, now only 30-50 nm.
  • APOB48 and APOE are important to identify the chylomicron remnant in the liver for endocytosis and breakdown.
  • FIG. 1 is a flowchart of a process of purifying APO from plasma fraction IV according to the present invention
  • FIG. 2 is a flowchart of another process of purifying APO from plasma fraction IV according to the present invention.
  • FIG. 3 is a flowchart of an AFCC process of purifying prothrombin complex from cryopaste in accordance with the present invention
  • FIG. 4 is a flowchart of an AFCC process of purifying prothrombin complex from fraction III in accordance with the present invention
  • FIG. 5 shows the electrophoresis result of cation chromatography of proteins including transferrin, human albumin, APOA1, PCC and A1AT;
  • FIG. 6 shows the 2D electrophoresis results of AFOD
  • FIG. 7 shows an analysis of a Fraction IV suspension by 2D electrophoresis
  • FIG. 10 is a graph showing the relative abundance over time of Q15 Gene Symbol ⁇ CASK Isoform 3 of Peripheral plasma membrane protein CASK ⁇ IFNA13 IFNA1 Interferon alpha-1/13;
  • FIG. 11 shows the results of a 2D electrophoresis of prothrombin complex concentrate
  • FIG. 12 shows the results of a 2D electrophoresis of Fraction III
  • FIG. 13 shows the results of a 2D electrophoresis of cryopaste
  • FIG. 14 is a flowchart of a process for purifying AFOD
  • FIG. 15 is a graph showing cancer cell proliferation during a 3-day in vitro study of colon and breast cancer cell lines in the presence of varying concentrations of AFOD solution;
  • FIG. 16 is an image taken on Day 3 after treatment showing the proliferation of Colon cancer cells HCT 116 in 0% AFOD solution;
  • FIG. 17 is an image taken on Day 3 after treatment showing the proliferation of Colon cancer cells HCT 116 in 2% AFOD solution;
  • FIG. 18 is an image taken on Day 3 after treatment showing the proliferation of Colon cancer cells HCT 116 in 10% AFOD solution;
  • FIG. 19 is an image taken on Day 3 after treatment showing the proliferation of Breast cancer cells MCF-7 in 0% AFOD solution
  • FIG. 20 is an image taken on Day 3 after treatment showing the proliferation of Breast cancer cells MCF-7 in 2% AFOD solution;
  • FIG. 21 is an image taken on Day 3 after treatment showing the proliferation of Breast cancer cells MCF-7 in 10% AFOD solution;
  • FIG. 22 is a graph showing cancer cell proliferation during a 3-day in vitro study of liver and pancreas cancer cell lines in the presence of varying concentrations of AFOD solution;
  • FIG. 23 is an image taken on Day 3 after treatment showing the proliferation of liver cancer cells HepG2 in 0% AFOD solution;
  • FIG. 24 is an image taken on Day 3 after treatment showing the proliferation of liver cancer cells HepG2 in 2% AFOD solution;
  • FIG. 25 is an image taken on Day 3 after treatment showing the proliferation of liver cancer cells HepG2 in 10% AFOD solution;
  • FIG. 26 is an image taken on Day 3 after treatment showing the proliferation of pancreas cancer cells PAC-1 in 0% AFOD solution;
  • FIG. 27 is an image taken on Day 3 after treatment showing the proliferation of pancreas cancer cells PAC-1 in 2% AFOD solution;
  • FIG. 28 is an image taken on Day 3 after treatment showing the proliferation of pancreas cancer cells PAC-1 in 10% AFOD solution;
  • FIG. 29 is a graph showing the proliferation of a variety of cancer cells over a 3-day trial period in the presence of varying concentrations of AFOD;
  • FIG. 30 shows the images of FIGS. 16-21 next to one another for comparison
  • FIG. 31 shows the images of FIGS. 23-28 next to one another for comparison
  • FIG. 32 is a graph showing cell proliferation during a 3-day in vitro study of cervical cancer cell line Hela in the presence of 16 distinct solutions, listed on the x axis.
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 33 contains 16 photographs taken on Day 3 after treatment, showing the proliferation of Cervical Cancer line Hela in the presence of 16 different solutions (listed on each photo).
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 34 is a graph showing cell proliferation during a 3-day In Vitro study of Gastric cancer cell AGS in the presence of 16 distinct solutions, listed on the x axis.
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 35 contains 16 photographs taken on Day 3 after treatment, showing the proliferation of Gastric Cancer Cell AGS in the presence of 16 different solutions (listed on each photograph).
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 36 is a graph showing cell proliferation during a 3-day In Vitro study of Breast Cancer Cell Line SK-BR-3 in the presence of 16 distinct solutions, listed on the x axis.
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 37 contains 9 photos taken on Day 3 after treatment, showing the proliferation of Breast Cancer Cell Line SK-BR-3 in the presence of different solutions (listed on each photograph).
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, and TB 5 U/mL;
  • FIG. 38 contains 7 photographs taken on Day 3 after treatment, showing the proliferation of Breast Cancer Cell Line SK-BR-3 in the presence of different solutions (listed on each photograph).
  • the solutions are AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 39 is a graph showing cell proliferation during a 3-day In Vitro study of Ovarian Cancer Cell Line SK-OV-3 in the presence of 16 distinct solutions, listed on the x axis.
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 40 contains 16 photographs taken on Day 3 after treatment, showing the proliferation of Ovarian Cancer Cell SK-OV-3 in the presence of 16 different solutions (listed on each photograph).
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 41 is a graph showing cell proliferation during a 3-day In Vitro study of Lung Adenocarcinoma Cell Line SPC-A-1 in the presence of 16 distinct solutions, listed on the x axis.
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 42 contains 16 photographs taken on Day 3 after treatment, showing the proliferation of Lung Adenocarcinoma Cell Line SPC-A-1 in the presence of 16 different solutions (listed on each photograph).
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 43 is a graph showing cell proliferation during a 3-day In Vitro study of Espohageal Cancer Cell Line TE-1 in the presence of 16 distinct solutions, listed on the x axis.
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 44 contains 16 photographs taken on Day 3 after treatment, showing the proliferation of Espohageal Cancer Cell Line TE-1 in the presence of 16 different solutions (listed on each photograph).
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 45 is a graph showing cell proliferation during a 3-day In Vitro study of Liver Cancer Cell Line BEL-7402 in the presence of 16 distinct solutions, listed on the x axis.
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 46 contains 16 photographs taken on Day 3 after treatment, showing the proliferation of Liver Cancer Cell Line BEL-7402 in the presence of 16 different solutions (listed on each photograph).
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 47 is a graph showing cell proliferation during a 3-day In Vitro study of Pancreas Cancer Cell Line PANC-1 in the presence of 16 distinct solutions, listed on the x axis.
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 48 contains 16 photographs taken on Day 3 after treatment, showing the proliferation of Pancreas Cancer Cell Line PANC-1 in the presence of 16 different solutions (listed on each photograph).
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 49 is a graph showing cell proliferation during a 3-day In Vitro study of Leukemia Cancer Cell Line Dami in the presence of 16 distinct solutions, listed on the x axis.
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 50 contains 16 photographs taken on Day 3 after treatment, showing the proliferation of Leukemia Cancer Cell Line Dami in the presence of 16 different solutions (listed on each photograph).
  • the solutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;
  • FIG. 51 is a graph showing the summary data for the proliferation of Leukemia Cells (Acute Promyelocytic Leukemia Cell T24) in the presence of 0% protein, 2% protein, and 10% protein of AFOD, and Bladder Cancer cells (Bladder Cancer Cell NB4) in the presence of 0% protein, 2% protein, and 10% protein of AFOD during the 3-day trial period.
  • Leukemia Cells Acute Promyelocytic Leukemia Cell T24
  • Bladder Cancer cells Bladder Cancer Cell NB4
  • FIG. 52 shows 6 pictures taken after the trial which show the proliferation of Leukemia Cells (Acute Promyelocytic Leukemia Cell T24) in the presence of 0% protein, 2% protein, and 10% protein of AFOD, and Bladder Cancer cells (Bladder Cancer Cell NB4) in the presence of 0% protein, 2% protein, and 10% protein of AFOD during the 3-day trial period.
  • Leukemia Cells Acute Promyelocytic Leukemia Cell T24
  • Bladder Cancer cells Bladder Cancer Cell NB4
  • FIG. 53 is a graph showing the summary data for the proliferation of Cervical Cancer Cells (Human Cervical Cancer Cell Line Hela) in the presence of a variety of solutions, listed on the x-axis, at 0%, 2%, and 10% concentrations of protein, respectively.
  • FIG. 54 is a graph showing the summary data for the proliferation of Gastric Cancer Cells (Human Gastric Cancer Cell Line AGS) in the presence of a variety of solutions, listed on the x-axis, at 0%, 2%, and 10% concentrations of protein, respectively.
  • FIG. 55 is a graph showing the summary data for the proliferation of Ovarian Cancer Cells (Human Ovarian Cancer Cell SK-OV-3) in the presence of a variety of solutions, listed on the x-axis, at 0%, 2%, and 10% concentrations of protein, respectively.
  • FIG. 56 is a graph showing the summary data for the proliferation of Breast Cancer Cells (Human Breast Cancer Cell Line SK-BR-3) in the presence of a variety of solutions, listed on the x-axis, at 0%, 2%, and 10% concentrations of protein, respectively.
  • FIG. 57 is a graph showing the summary data for the proliferation of Esophageal Cancer Cells (Human Esophageal Cancer Cell Line TE-1) in the presence of a variety of solutions, listed on the x-axis, at 0%, 2%, and 10% concentrations of protein, respectively.
  • FIG. 58 is a graph showing the summary data for the proliferation of Liver Cancer Cells (Human Liver Cancer Cell Line BEL-7402) in the presence of a variety of solutions, listed on the x-axis, at 0%, 2%, and 10% concentrations of protein, respectively.
  • FIG. 59 is a graph showing the summary data for the proliferation of Lung Cancer Cells (Lung Adenocarcinoma Cell Line SPC-A-1) in the presence of a variety of solutions, listed on the x-axis, at 0%, 2%, and 10% concentrations of protein, respectively.
  • FIG. 60 is a graph showing the summary data for the proliferation of Pancreas Cancer Cells (Human Pancreas Cancer Cell Line PANC-) in the presence of a variety of solutions, listed on the x-axis, at 0%, 2%, and 10% concentrations of protein, respectively.
  • FIG. 61 is a graph showing the summary data for the proliferation of Leukemia Cells (Human Lymphocyte Leukemia Cell Line Jurkat) in the presence of a variety of solutions, listed on the x-axis, at 0%, 2%, and 10% concentrations of protein, respectively.
  • Leukemia Cells Human Lymphocyte Leukemia Cell Line Jurkat
  • FIG. 62 is a photograph of five sample vials of bacteria during a microbe test with AFOD RAAS 1 on Staphylococcus aureus , from left to right, having 8 mL AFOD added, having 10 mL AFOD added, having 12 mL AFOD added, a positive control, and a negative control.
  • FIG. 63 is a series of photographs of three sample vials of bacteria, taken at different times during a microbe test of AFOD on Staphylococcus aureus.
  • FIG. 64 is a series of photographs of five sample vials of bacteria, taken at different times during a microbe test of AFCC on Staphylococcus aureus.
  • FIG. 65 is a photograph showing the aorta of a lab animal given a high fat diet after 10 weeks, with a plaque area of 24.3%.
  • FIG. 66 is a photograph showing the liver tissue (with fat deposits) of a lab animal after 10 weeks of a high fat diet.
  • FIG. 67 is a photograph showing the aorta of a lab animal without AFOD RAAS 1 and then a normal diet for 4 weeks, with a plaque area of 45.3%.
  • FIG. 68 is a photograph showing the aorta of a lab animal without AFOD RAAS 1 and then a normal diet for 8 weeks, with a plaque area of 98.5%.
  • FIG. 69 is a photograph showing the aorta of a lab animal without AFOD RAAS 1 and then a normal diet for 8 weeks, with a plaque area of 78.94%.
  • FIGS. 70-76 is a photograph of a container having a mixture of a product with a yellow color and a product with a blue that, unlike yellow and blue chemicals, will not turn green.
  • FIG. 77 is a photograph showing an artery of a lab animal is given a normal diet for 8 weeks.
  • FIG. 78 is a photograph showing the aortas of two lab animals tested by AFOD RAAS 1, the aortas having a plaque area of 0.
  • FIG. 79 is a photograph showing the buildup of plaque to a plaque area of 13.29% in the aorta of a lab animal with AFOD RAAS 1-A1 for 8 weeks.
  • FIG. 80 is a photograph showing the buildup of plaque to a plaque area of 20.5% in the aorta of a lab animal with AFOD RAAS 1-A1 for 8 weeks.
  • FIG. 81 is a photograph showing the buildup of plaque to a plaque area of 58.4% in the aorta of a lab animal with AFOD RAAS 1.
  • FIG. 82 is a photograph showing the buildup of plaque to a plaque area of 82.17% in the aorta of a lab animal with AFOD RAAS 1.
  • FIG. 83 is a photograph showing the buildup of plaque to a plaque area of 47.27% in the aorta of a lab animal with AFOD RAAS 1 for 11 weeks.
  • FIG. 84 is a photograph showing the buildup of plaque to a plaque area of 40.32% in the aorta of a lab animal with AFOD RAAS 1 for 11 weeks.
  • FIG. 85 is a photograph showing the buildup of plaque to a plaque area of 51.13% in the aorta of a lab animal with AFOD RAAS 1 for 11 weeks.
  • urea is no longer required but need 2 steps of chromatography, as is shown in FIG. 1 .
  • Nr 5 to Nr 8 can be processed separately and put together at the Non Sterile Final Bulk-Sterile Filtration-Filling-Final Products.
  • the resulted suspension was then treated with Tween-80 and TNBP for virus inactivation at 25 C for 6 hours, 6.
  • the resulted suspension was adjusted pH and ionic strength and then subjected to a canion chromatography like DEAE.
  • the targeted proteins were then binding to the canion chromatography resin, which are transferrin, human albumin, APO and A1AT.
  • the 1 st elution was salt solution to elude the transferrin.
  • the 2 nd elution was then eluded by a high concentration salt solution, which was APO.
  • the 3 rd eluted fraction was human albumin by a low pH solution.
  • Finally the 4 th elution was A1AT which was eluted by a high concentration salt solution. 7.
  • the resulted various elution was then subjected to different chromatography for further purification to achieve a high purity.
  • the 1 st elution fraction was subjected to a CM chromatography.
  • the 2 nd elution fraction was subjected to a butyl chromatography.
  • the 3 rd elution fraction was subjected to a blue chromatography.
  • the 4 th elution fraction was subjected to a blue chromatography and a subsequent butyl chromatography.
  • the resulted protein fractions were then dialyzed and concentrated. The pH was adjusted and stabilizer was then added.
  • the resulted protein solutions were subjected to DV20 filtration for virus removal except human albumin. 10.
  • the human albumin could be virus inactivated by Double pasteurization.
  • the resulted transferrin, APO, human albumin and A1AT can be filled.
  • AFCCRAAS 1 These processes of protein containing Healthy Good cells in Process 1 and Process 3 below are specially designed for Hemophilia A,B and WvB who have Been infected by HBV, HCV and specially HIV during the early of 1980 when effective process of inactivation of Enveloped viruses has not been introduced.
  • Process to separate Factor II, VII, IX, and X Process to separate Factor II, VII, IX, and X (ProthoRAAS®)+Human Albumin (AlbuRAAS®)+Immunoglobulin (GammaRAAS) 3.
  • Process to separate Factor II, VII, IX and X from Cryopaste 4. Process to separate Factor II, VII, IX and X from Cryopaste+ATA1 APO+Human Albumin (AlbuRAAS®) and Immunoglobulin (GammaRAAS) 5.
  • Process to separate Thrombin (ThrombiRAAS®) from Fraction III Process to combine all protein from Fraction III.
  • AFOD High density Lipoprotein (ApoA1):
  • FIGS. 5 and 6 The three dots in our analysis of AFOD are all ApoA1. The difference showed in 2D electropherosis of FIG. 6 might be due to different isoform of ApoA1 or Apo in the Apo family.
  • Fraction IV suspension The main proteins found in Fraction IV suspension are:
  • SEMENOGELIN-1 The protein encoded by this gene is the predominant protein in semen
  • HAPTOGLOBIN In Blood Plasma, Haptoglobin binds free hemoglobin (Hb) released from erythrocytes with high affinity and thereby inhibits its oxidative activity.
  • VIMENTIN is a member of the intermediate filament family of proteins that is especially found in connective tissue. They, along with microtubules and actin microfilaments, make up the cytoskeleton
  • THE NESPRINS are a family of proteins that are found primarily in the outer nuclear membrane. Nesprin-1 and Nesprin-2 bind to actin filaments.
  • VITAMIN-D BINDING PROTEIN belongs to the albumin gene family, together with Human serum albumin and alpha-fetoprotein. It is a multifunctional protein found in plasma, ascetic fluid, cerebrospinal fluid and on the surface of many cell types. It binds to Vitamin D and its plasma metabolites and transport them to target tissues.
  • CASK PROTEIN Peripheral plasma membrane protein CASK is a protein that in humans is encoded by the CASK gene. This protein is a multi domain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking. It interacts with the transcription factor TBR1 and binds to several cell-surface proteins including amyloid precursor protein, neurexins, and syndecans.
  • FIG. 10 relates to Q15 Gene Symbol ⁇ CASK Isoform 3 of Peripheral plasma membrane protein CASK ⁇ IFNA13; IFNA1 Interferon alpha-1/13
  • AFCC is Prothombin Complex Concentrate (ProthoRAAS®) a combination of blood clotting factors II, VII, IX and X or Factor IX.
  • Factor IX is one of several factors made in the liver with similar structural properties.
  • factor IX antihaemophilic factor B
  • PPSB factors prothombin complex group of factors
  • the proteins in this group are usually isolated together in fraction III in the Cohn alcohol fractionation process.
  • PCC Prothombin complex concentrates
  • Liver disease acute and chronic—active hepatitis, cirrhosis
  • Vitamin K deficiency Oral anticoagulants, Obstructive jaundice, Malabsorption, changes in intestinal flora(antibiotics, Morbus Crohn, ulcerative colitis)
  • Fraction III like Fraction IV contains a lot more of proteins other than Thrombin, Prothombin Complex, as can be seen in FIG. 12 . All these proteins are also being identified.
  • Electropherosis of Cryopaste results also show some other proteins which are being indentified Beside Fibrinogen and Factor VIII, as can be seen in FIG. 13 .
  • the 1 St 200 g AFOD was purified in East China University of Science and Technology using Process Nr 1, a flow chart for which is presented in FIG. 14 .
  • the pilot production capability of that lab is about 5 kg per time.
  • the purification process was modified according to their equipments on site but the flow was same as we have done in this Dec. The major differences are as following
  • the resulted AFOD was about 200 g for total 10 lots and all of AFOD were lyophilized.
  • the stabilizer used was mannitol and this product has been used to perform clinical studies on 52 rabbits in summer of 2008.
  • AFCC RAAS 1 A current product of Shanghai RAAS Blood products Co Ltd approved for Sales in China and has been exported to a certain country around the globe. Product has been manufactured at large industrial scale.
  • the antibiotics added in cell culture medium is basically to prevent the potential bacterial or fugal contamination during the culture.
  • the antibiotics they added contains penicillin, streptomycin, and amphotericin B. Basically it won't kill cell and it is a routine recipe in animal cell culture. And they also include a control in which cells are cultured with DMEM/FBS/antibiotics only.
  • FIGS. 15-28 Reference is made to FIGS. 15-28 .
  • the dose dependent cell killing effect of AFOD by CCK8 assay is shown in FIG. 29 .
  • FIGS. 30 and 31 Pictures of the cancer cells are shown in FIGS. 30 and 31 .
  • Cancer cell line Human colon cancer cell line (HCT-116), Human Breast cancer cell line (MCF-7), Human liver cancer cell line (HepG2), Human pancreatic cancer cell line (PAC-1) 2.
  • CCK 8 cell counting kit-8): Dojindo molecular technologies, Inc (Maryland, US), product code #CK04-11 3.
  • Cell culture medium
  • FIGS. 32-61 FURTHER IN VITRO STUDIES of MORE CANCERS CELL LINES are shown in FIGS. 32-61 .
  • FIGS. 62-64 Reference is made to FIGS. 62-64 .
  • HCV, HIV1,2 and HBsAg on the left are Elisa testing HCV-RNA HIVRNA
  • HBV DNA are results of NAT Testing at Shanghai RAAS NAT Laboratory for A total of units of plasma 2,486,188 during five years period from 2006 to 2010.
  • 241 Tested positive HCV by Elisa Confirmed HCV Positive by NAT is only 5 units so a total of 236 units are FALSE POSITIVE by Elisa Method. From 2007 to 2010 there is NO HCV POSITIVE from our donor Population therefore
  • NAT Lab has diluted the positive plasma sample to weaken the presence of HIV1,2 virus to the level of 1:3200 and the first test result is as below for the HIV Positive Plasma to use as A CONTROL.
  • the rabbits were fed with normal diet under regular lab conditions for 5-10 days. The rabbits were fasted for 12 hrs before the beginning of the experiments. Blood parameters were then tested as the normal level of plasma indicators. The animals were then randomly grouped for the experiment.
  • mice After grouping of the experimental animals, they were switched to high-fat diet. Body weight and plasma parameters were tested and recorded once every two weeks until indicators shown to have lipid metabolism disorders and the formation of obvious fatty streak lesions in blood vessels. The animals were switched from high-fat diet to normal diet. These are the grouping of the experimental animals: (1) positive control group, (2) AFOD RAAS 1-A1 treatment group was further divided into high, medium and low three dose sub-groups. During the first 4 weeks of the AFOD RAAS 1—treatment, plasma parameters and animal general conditions were carefully monitors and recorded. At the end of the experiments, the lab animals were sacrificed for pathological and anatomical analysis.
  • Control groups build up the animal models, without AFOD RAAS 1, then normal diet for 8 weeks).
  • VLDL- TC/ Weight TG TCH C HDL-C LDL-C HDL-C Start 2.2 0.93 1.430 0.958 0.432 0.472 4.185 Before 2.45 4.507 34.683 15.443 10.168 19.24 3.667 After 2.65 1.94 3.322 1.14 1.17 2.19 3.844 3) Positive control (crestol, administered 4 weeks)
  • the invention reveals that all healthy good cells have eaten all fats (BAD CELLS and damaged cells as described in the function of the liver not through the formation of HDL.
  • the Inventor has found that even with the longer And higher dosage of AFOD RAAS 1Group 2, the formation of HDL has been reduced to 54.15% from 92.36% of AFODRAAS 1 Group 1 and the Total of TC/HDL-C is ⁇ 53.55% much higher than to compare with AFODRAAS 1 Group 2 which has TC/HDL-C ⁇ 40.48%
  • Atorvastatin® was also used in this study when comparing with control group, it has significantly reduced TG ⁇ 60.73% and increased HDL to 64.69% however TCH have increased to 61.74%, VLDL-C increased 87.40% LDL-C increased 46.56% and TC/HDL-C is 5.47%. In conclusion it can reduces TG and increases HDL but will NOT LOWER Bad Cholesterol VLDL-C, LDL
  • Atorvastatin® cannot remove FATS from PLAQUE whereas AFODRAAS1 and AFCCRAAS1 CAN REMOVE FATS from PLAQUE, CLEAN the arteries.
  • FIGS. 70-76 Reference is made to FIGS. 70-76 .
  • ATORVASTATIN® is one among thousands of drugs available can be combined with AFODRAAS1-85 or AFCC RAAS1-85 to enhance the EFFICACY of the drugs.
  • Drugs like ATORVASTATIN® and LIPITOR® have helped a lot of people with HIGH CHOLESTEROL.
  • liver surface When the animal models were first made, the liver surface of the lab animals from the animal-model group showed abnormal white colored spots. Histological analysis showed that it is???. The surface of the liver feels harder than normal tissue. The liver samples taken from the -Al treated group has fewer???. The surface is not as tough as when the animal model was first made. The un-treated group also showed relief in the??? and softened. The probable reason is that because the high cholesterol and atherosclerosis model is made in a short period of time, the switch to normal diet also helped to relief the symptoms. 2) Liver index
  • the liver index did not show any changes after the AFOD RAAS 1 treatment.
  • Atorvastatin® cannot remove FATS from PLAQUE whereas AFODRAAS1-85 and AFCCRAAS1-85 CAN REMOVE FATS from PLAQUE, CLEAN the arteries.
  • FIGS. 79 and 80 show build up the animal models, with AFOD RAAS 1-A1 8 weeks.
  • FIGS. 81 and 82 show build up the animal models, with AFOD RAAS 1 8 weeks (another rabbit).
  • FIGS. 83-85 show Group with AFOD RAAS 1 11 weeks.
  • Wk0, wk10 and wk18 mean the actual value of each parameter.
  • Wk18-wk0 or wk21-wk0
  • Wk18-wk10 or wk21-wk10) means the change calculated by comparing the value of wk18 (or wk21) to the value of wk 10.

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US13/114,951 2007-09-19 2011-05-24 Manufacturing and Purification Processes of Complex Protein found in Fraction IV to make a separated Apo, Transferrin , and Alpha 1 Anti strepsin (A1AT) or A combined Transferrin / Apo/Human Albumin/A1AT and all new found proteins Abandoned US20120177610A1 (en)

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US13/114,951 US20120177610A1 (en) 2007-09-19 2011-05-24 Manufacturing and Purification Processes of Complex Protein found in Fraction IV to make a separated Apo, Transferrin , and Alpha 1 Anti strepsin (A1AT) or A combined Transferrin / Apo/Human Albumin/A1AT and all new found proteins
PCT/US2011/038595 WO2012121740A1 (fr) 2011-03-04 2011-05-31 Processus de fabrication et de purification de protéines complexes trouvées dans la fraction 4
PCT/US2011/038679 WO2012121742A1 (fr) 2011-03-04 2011-06-01 Joint de fibrine (fibringluraas®) constitué d'un kit de fibrinogène lyophilisé fortement concentré intentionnellement enrichi et conservé avec l'inhibiteur de fibrinolyse a1at
TW104101525A TWI600661B (zh) 2011-03-04 2012-03-03 製造個別的載脂蛋白、轉鐵蛋白及阿法１抗胰蛋白酶（ａ１ａｔ）或組合的轉鐵蛋白／載脂蛋白／人類白蛋白／ａ１ａｔ及所有新發現的蛋白質之第ｉｖ部分中發現的複合蛋白之製備及純化方法
TW101107176A TWI508972B (zh) 2011-03-04 2012-03-03 製造個別的載脂蛋白、轉鐵蛋白及阿法１抗胰蛋白酶（ａ１ａｔ）或組合的轉鐵蛋白／載脂蛋白／人類白蛋白／ａ１ａｔ及所有新發現的蛋白質之第ｉｖ部分中發現的複合蛋白之製備及純化方法
TW101107169A TW201309719A (zh) 2011-03-04 2012-03-03 由故意增富且保留纖維蛋白分解抑制劑ａ１ａｔ之冷凍乾燥的高濃縮纖維蛋白原套組所構成之纖維蛋白密封劑（ｆｉｂｒｉｎｇｌｕｒａａｓ®）
TW104101523A TWI610938B (zh) 2011-03-04 2012-03-03 製造個別的載脂蛋白、轉鐵蛋白及阿法１抗胰蛋白酶（ａ１ａｔ）或組合的轉鐵蛋白／載脂蛋白／人類白蛋白／ａ１ａｔ及所有新發現的蛋白質之第ｉｖ部分中發現的複合蛋白之製備及純化方法
US14/056,363 US9649366B2 (en) 2007-09-19 2013-10-17 Manufacturing and purification processes of Complex protein found in Fraction IV to make a separated Apo, Transferrin, and Alpha 1 Antitrypsin (A1AT) or a combined Transferrin/Apo/Human Albumin/A1AT and all new found proteins
US14/056,410 US20140140987A1 (en) 2008-07-15 2013-10-17 Manufacturing and Purification Processes of Complex Protein found in Fraction IV to make a separated Apo, Transferrin, and Alpha 1 Anti strepsin (A1AT) or A combined Transferrin/Apo/Human Albumin/A1AT and all new found proteins

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PCT/US2007/020258 WO2008088403A2 (fr) 2006-12-20 2007-09-19 Procédé de purification de l'apolipoprotéine a-1
US99020308A 2008-07-15 2008-07-15
US12/457,796 US8013122B2 (en) 2006-12-20 2009-06-22 Method of purifying apolipoprotein A-1
US201113064070A 2011-03-04 2011-03-04
US201161457380P 2011-03-14 2011-03-14
US201161452860P 2011-03-15 2011-03-15
US201161472930P 2011-04-07 2011-04-07
US13/108,970 US20120195953A1 (en) 2007-09-19 2011-05-16 Fibrin sealant (FIBRINGLURAAS) consisting of a kit of lyophilized high concentrate fribinogen intentionally enriched and preserved with fibronolysis inhibitor A1AT
US13/114,951 US20120177610A1 (en) 2007-09-19 2011-05-24 Manufacturing and Purification Processes of Complex Protein found in Fraction IV to make a separated Apo, Transferrin , and Alpha 1 Anti strepsin (A1AT) or A combined Transferrin / Apo/Human Albumin/A1AT and all new found proteins

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US13/108,970 Continuation-In-Part US20120195953A1 (en) 2007-09-19 2011-05-16 Fibrin sealant (FIBRINGLURAAS) consisting of a kit of lyophilized high concentrate fribinogen intentionally enriched and preserved with fibronolysis inhibitor A1AT

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US14/056,363 Division US9649366B2 (en) 2007-09-19 2013-10-17 Manufacturing and purification processes of Complex protein found in Fraction IV to make a separated Apo, Transferrin, and Alpha 1 Antitrypsin (A1AT) or a combined Transferrin/Apo/Human Albumin/A1AT and all new found proteins

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US14/056,410 Abandoned US20140140987A1 (en) 2008-07-15 2013-10-17 Manufacturing and Purification Processes of Complex Protein found in Fraction IV to make a separated Apo, Transferrin, and Alpha 1 Anti strepsin (A1AT) or A combined Transferrin/Apo/Human Albumin/A1AT and all new found proteins
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US14/056,363 Active 2028-01-13 US9649366B2 (en) 2007-09-19 2013-10-17 Manufacturing and purification processes of Complex protein found in Fraction IV to make a separated Apo, Transferrin, and Alpha 1 Antitrypsin (A1AT) or a combined Transferrin/Apo/Human Albumin/A1AT and all new found proteins

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CN106519007A (zh) * 2016-12-12 2017-03-22 王家祥 一种单链多肽及其在制备用于预防和治疗胃癌的药物中的应用

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US20140140987A1 (en) 2014-05-22
WO2012121742A1 (fr) 2012-09-13
TW201514196A (zh) 2015-04-16
TW201514199A (zh) 2015-04-16
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