NL8302324A - New escherichia coli strain contg. hybrid plasmid - coding for insulin-like growth factor in form of new precursor - Google Patents
New escherichia coli strain contg. hybrid plasmid - coding for insulin-like growth factor in form of new precursor Download PDFInfo
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- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 title claims abstract description 25
- 241000588724 Escherichia coli Species 0.000 title claims abstract description 13
- 239000013612 plasmid Substances 0.000 title claims abstract description 11
- 239000002243 precursor Substances 0.000 title claims abstract description 8
- 102000013275 Somatomedins Human genes 0.000 title abstract description 5
- 102000004218 Insulin-Like Growth Factor I Human genes 0.000 claims description 16
- 241000894006 Bacteria Species 0.000 claims description 3
- 230000001737 promoting effect Effects 0.000 claims description 3
- 238000002360 preparation method Methods 0.000 claims description 2
- 239000013543 active substance Substances 0.000 claims 1
- 239000001963 growth medium Substances 0.000 claims 1
- 238000004519 manufacturing process Methods 0.000 claims 1
- 239000002299 complementary DNA Substances 0.000 abstract description 6
- 210000005229 liver cell Anatomy 0.000 abstract description 3
- 102100034343 Integrase Human genes 0.000 abstract 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 abstract 1
- 125000003275 alpha amino acid group Chemical group 0.000 abstract 1
- 108020004999 messenger RNA Proteins 0.000 abstract 1
- 230000001131 transforming effect Effects 0.000 abstract 1
- 150000001413 amino acids Chemical group 0.000 description 7
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 108020004635 Complementary DNA Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- 238000000034 method Methods 0.000 description 2
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- CUJRVFIICFDLGR-UHFFFAOYSA-N acetylacetonate Chemical compound CC(=O)[CH-]C(C)=O CUJRVFIICFDLGR-UHFFFAOYSA-N 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- -1 phosphate triester Chemical class 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
Classifications
-
- 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
- C07K14/575—Hormones
- C07K14/65—Insulin-like growth factors, i.e. somatomedins, e.g. IGF-1, IGF-2
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- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Endocrinology (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Diabetes (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Abstract
Description
£ - _ . Λ % $£ - _. Λ% $
Als uitvinders zijn genoemd Drs. M. Jansen,Drs. M. Jansen,
Prof. Dr. J.L. van den Brande, Prof. Dr. Ir.Prof. Dr. J.L. van den Brande, Prof. dr. Dr. Ir.
J.S. Sussenbach.J.S. Sussenbach.
Escherichia coli stam, een voor deze stam karakteristiek plasmide, een werkwijze ter bereiding van dit plasmide, een precursor van een somatomedine, alsmede een groeibevor-5 derend preparaat.Escherichia coli strain, a plasmid characteristic of this strain, a method of preparing this plasmid, a precursor of a somatomedin, as well as a growth promoting preparation.
De uitvinding betreft een Escherichia coli stam, waaraan de naam E. coli pIGF-I werd gegeven, met een 10 plasmide, welke het mogelijk maakt via de recombinant-DNA- technieken de groeifaktor IGF-I op grote schaal te produceren.The invention relates to an Escherichia coli strain, which was given the name E. coli pIGF-I, with a plasmid which makes it possible to produce the growth factor IGF-I on a large scale via the recombinant DNA techniques.
Somatomedines of insulineachtige groeifak-toren (IGF) vormen een heterogene groep peptiden met sterke groei bevorderende effekten, zowel in vitro (zie Clemmons, D.Somatomedins or insulin-like growth factors (IGF) form a heterogeneous group of peptides with strong growth promoting effects both in vitro (see Clemmons, D.
15 R. & Van Wijk, J.J., J. Cell Phys. 106, 361-367 (1981)), als in vivo (zie Schoenle, E c.s., Nature 296, 252-253 (1982)).R. & Van Wijk, J.J., J. Cell Phys. 106, 361-367 (1981)), as in vivo (see Schoenle, E et al., Nature 296, 252-253 (1982)).
Van een van deze faktoren, namelijk het IGF-I is de aminozuurvolgorde volledig bekend (zie Rinderknecht, E & Humbel, R.E., FEBS Lett. 89, 283-286 (1978).The amino acid sequence of one of these factors, namely the IGF-I, is fully known (see Rinderknecht, E & Humbel, R.E., FEBS Lett. 89, 283-286 (1978).
20 In figuur 1 is de aminozuurvolgorde van het IGF-I molekuul terug te vinden in het onderstreepte gedeelte.Figure 1 shows the amino acid sequence of the IGF-I molecule in the underlined section.
Daaruit blijkt dat IGF-I is opgebouwd uit 70 aminozuren in de aangegeven volgorde te beginnen met Glycine (Gly) en eindigende met alanine (Ala). Aangezien het aantal aminozuurbouwstenen 25 zo groot is, is het nagenoeg uitgesloten, IGF-I organisch- synthetisch op een economisch verantwoorde wijze te bereiden.This shows that IGF-I is made up of 70 amino acids in the order given, starting with Glycine (Gly) and ending with alanine (Ala). Since the number of amino acid building blocks is so great, it is practically impossible to prepare IGF-I organosynthetically in an economically responsible manner.
De uitvinding opent nu de mogelijkheid IGF-I op grote schaal te produceren via recombinant-DNA-technieken.The invention now opens the possibility of producing IGF-I on a large scale via recombinant DNA techniques.
______' ^ 8302324 - 2 -______ '^ 8302324 - 2 -
Gevonden werd namelijk een.E. coli stam (E. coli pIGF-I), die een plasmide pIGF-I bezit, waarvan een deel van de nucleotidesequentie is weergegeven in figuur 1.A E. was found. coli strain (E. coli pIGF-I), which has a plasmid pIGF-I, part of the nucleotide sequence of which is shown in Figure 1.
Het onderstreepte gedeelte van deze nucleotidevolgorde corres-5 pondeert met de volledige aminozuurvolgorde van IGF-I. De nucleotidevolgorde weergegeven in figuur 1 toont verder, dat IGF-I in de humane cel als precursor wordt gemaakt (verderop aangeduid als pre IGF-I).The underlined portion of this nucleotide sequence corresponds to the full amino acid sequence of IGF-I. The nucleotide sequence shown in Figure 1 further shows that IGF-I is made as a precursor in the human cell (hereinafter referred to as pre IGF-I).
De vondst van de stam van E. coli pIGF-I 10 betekent een belangrijke stap voorwaarts naar een economisch verantwoorde bereiding van de groei bevorderende faktor IGF-I. Daaraan bestaat behoefte zowel voor geneeskundige doeleinden als ter vervanging van het dure kalverserum, dat thans wordt gebruikt voor weefselkweekdoeleinden.The discovery of the strain of E. coli pIGF-I 10 represents an important step forward towards an economically responsible preparation of the growth promoting factor IGF-I. There is a need for both medical purposes and to replace the expensive calf serum currently used for tissue culture purposes.
15 De bovengenoemde E. coli pIGF-I, gedeponeerd onder nr. CBS 45383 bij het Centraal Bureau voor Schimmelcultures te Baarn (Nederland) werd als volgt verkregen.The above-mentioned E. coli pIGF-I, deposited under no. CBS 45383 at the Central Bureau of Mold Cultures in Baarn (Netherlands), was obtained as follows.
Uitgegaan werd van een zogenaamde complementaire DNA-bibliotheek (kort aangeduid als cDNA; zie Woods, 20 D.E. et al. Proc. natn. Acac. Sci. USA 79, 5661-5665 (1982)), die als volgt tot stand kwam:A so-called complementary DNA library (briefly referred to as cDNA; see Woods, 20 D.E. et al. Proc. Natn. Acac. Sci. USA 79, 5661-5665 (1982)) was started as follows:
Een mengsel van zgn. "messenger" RNA’s uit de levercellen van een volwassen mens werd met behulp van het enzym reversed transcriptase omgezet in een mengsel van cDNA's. Met behulp van 25 "dG-dC tailing" werden deze cDNA's in het plasmide p KT 218 gezet. Hierna werd de bacterie E. coli K12Mc1061 met de cDNA bevattende plasmiden getransformeerd. Daardoor ontstond een verzameling van ca. 230.000 verschillende transformanten van de uitgangs E. coli, welke genetische informatie bevatten, 30 corresponderend met de verschillende "messenger" RNA's afkomstig uit menselijke levercellen.A mixture of so-called "messenger" RNAs from the liver cells of an adult human was converted into a mixture of cDNAs using the enzyme reversed transcriptase. These cDNAs were put into the plasmid p KT 218 using "dG-dC tailing". After this, the bacterium E. coli K12Mc1061 was transformed with the cDNA containing plasmids. This resulted in a collection of approximately 230,000 different transformants of the starting E. coli containing genetic information corresponding to the different "messenger" RNAs from human liver cells.
Ca. 60.000. van deze transformanten werden gescreend met synthetische oligonucleotiden. Daartoe werden uit de aminozurenvolgorde van IGF-I de reeks aminozuren op 35 de plaatsen 58 tot en met 62 (Glu-Met-Tyr-Cys-Ala) uitgekozen 8302324 ‘ < _ -s - 3 - « voor de synthese van. de overeenkomstige nucleotidevolgorde.Approx. 60,000. of these transformants were screened with synthetic oligonucleotides. To this end, from the amino acid sequence of IGF-I, the amino acid sequence at positions 58 to 62 (Glu-Met-Tyr-Cys-Ala) was selected 8302324 "<_ -s - 3 -" for the synthesis of. the corresponding nucleotide sequence.
Een mengsel van alle 8 mogelijke tetradecamere oligonucleo- tiden (5 T-G-A- ^ -A-T-G-T-A- § -T-G- § -G-C-3’) werd langs chemische weg gesynthetiseerd onder gebruikmaking van de 5 "solid phase" fosfaattriestermethode (zie Beaucage, S.L., &A mixture of all 8 possible tetradecamere oligonucleotides (5 TGA- ^ -ATGTA-§-TG-§-GC-3 ') was synthesized chemically using the 5 solid phase phosphate triester method (see Beaucage, SL, &
Caruthers, M.H., Tetrahedron Letters 22, 1859-1862 (1981)).Caruthers, M.H., Tetrahedron Letters 22, 1859-1862 (1981)).
De oligonucleotiden van het verkregen mengsel werden op de S’-plaats van een radioaktieve label voorzien met behulp van 32 polynucleotidekinase en P-adenosinetrifosfaat, waarna 10 ze werden gebruikt voor het screenen van de cDNA-bibliotheek volgens de koloniehybridisatiemethode van Grunstein en Hogness (Proc. natn. Acad. Sci. USA 72, 3961-3965 (1975). Twintig kolonies vertoonden hybridisatie met de gelabelde oligonucleotiden. Deze werden opnieuw met hetzelfde oligonuclectide-15 mengsel gescreend, waardoor 5 kolonies met ondubbelzinnige hybridisatie uiteindelijk geïsoleerd konden worden. Bij een analyse van de nucleotidevolgorde van het cDNA van een dezer kolonies volgens Maxam en Gilbert (Proc. natn. Acad. Sci. USA 74, 560-564 (1977)) bleek deze een stuk cDNA te bevatten van 20 777 nucleotiden waarvan de volledige volgorde is weergegeven in figuur 1.The oligonucleotides of the resulting mixture were radiolabeled at the S 'site using 32 polynucleotide kinase and β-adenosine triphosphate and used to screen the cDNA library by the colony hybridization method of Grunstein and Hogness (Proc Natn Acad Sci USA 72, 3961-3965 (1975) Twenty colonies showed hybridization with the labeled oligonucleotides, which were screened again with the same oligonuclectide mixture, ultimately allowing 5 colonies with unambiguous hybridization to be isolated. analysis of the nucleotide sequence of the cDNA from one of these colonies according to Maxam and Gilbert (Proc. natn. Acad. Sci. USA 74, 560-564 (1977)) it was found to contain a piece of cDNA of 20 777 nucleotides of which the complete sequence is shown in figure 1.
Deze nucleotidevolgorde geeft aan, dat IGF-I als precursor wordt gemaakt. ïïit deze precursor kan desgewenst IGF-I op een op zichzelf bekende wijze worden af-25 gesplitst. Voor de groeibevordering kunnen zowel de precursor als vrij IGF-I worden benut.This nucleotide sequence indicates that IGF-I is made as a precursor. If desired, IGF-I can be cleaved from this precursor in a manner known per se. Both precursor and free IGF-I can be used for growth promotion.
Door de vondst van de stam E. coli pIGF-I kan men door vermenigvuldiging van deze stam door deze te laten groeien op een daartoe geschikt medium de voor verder 30 onderzoek gewenste hoeveelheden cDNA coderend voor IGF-I en zijn precursor bereiden.By finding the strain E. coli pIGF-I, by multiplying this strain by growing it on an appropriate medium, it is possible to prepare the amounts of cDNA encoding IGF-I and its precursor desired for further investigation.
Een geschikt medium voor deze kweek is Lr Broth medium, bestaande uit per 1: 10 g bacto-trypton, 5 g bacto gistextrakt, 10 g NaCl, pH 7,5. De bakterien kunnen bij 33 -20°C worden bewaard in L-Browth/glycerol 1:1.A suitable medium for this culture is Lr Broth medium, consisting of 1: 10 g bacto-tryptone, 5 g bacto yeast extract, 10 g NaCl, pH 7.5. The bacteria can be stored at 33 -20 ° C in L-Browth / glycerol 1: 1.
8302324 . - 4 - 08302324. - 4 - 0
Uit de bacteriën kan men het plasmide op een gebruikelijke wijze isoleren (zie bijvoorbeeld het boek: Molecular Cloning, Ed.: T. Maniatis et al, 1982: Cold Spring Harbor Laboraty).The plasmid can be isolated from the bacteria in a conventional manner (see, for example, the book: Molecular Cloning, Ed .: T. Maniatis et al, 1982: Cold Spring Harbor Laboraty).
5 83023245 8302324
Claims (5)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| NL8302324A NL8302324A (en) | 1983-06-30 | 1983-06-30 | New escherichia coli strain contg. hybrid plasmid - coding for insulin-like growth factor in form of new precursor |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| NL8302324 | 1983-06-30 | ||
| NL8302324A NL8302324A (en) | 1983-06-30 | 1983-06-30 | New escherichia coli strain contg. hybrid plasmid - coding for insulin-like growth factor in form of new precursor |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NL8302324A true NL8302324A (en) | 1985-01-16 |
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NL8302324A NL8302324A (en) | 1983-06-30 | 1983-06-30 | New escherichia coli strain contg. hybrid plasmid - coding for insulin-like growth factor in form of new precursor |
Country Status (1)
| Country | Link |
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| NL (1) | NL8302324A (en) |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0189481A4 (en) * | 1984-07-13 | 1987-01-10 | Chiron Corp | Insulin-like Growth factor II. |
| EP0406913A1 (en) * | 1983-08-10 | 1991-01-09 | Amgen Inc. | Microbial expression of insulin-like growth factor |
| US5070075A (en) * | 1986-01-07 | 1991-12-03 | Washington University | Human preproinsulin-like growth factor I |
| US6331609B1 (en) | 1983-06-06 | 2001-12-18 | Genentech, Inc. | Preparation of human IGF via recombinant DNA technology |
-
1983
- 1983-06-30 NL NL8302324A patent/NL8302324A/en unknown
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6331609B1 (en) | 1983-06-06 | 2001-12-18 | Genentech, Inc. | Preparation of human IGF via recombinant DNA technology |
| US6331414B1 (en) | 1983-06-06 | 2001-12-18 | Genentech, Inc. | Preparation of human IGF via recombinant DNA technology |
| USRE39355E1 (en) * | 1983-06-06 | 2006-10-17 | Genetech, Inc. | Preparation of human IGF via recombinant DNA technology |
| EP0406913A1 (en) * | 1983-08-10 | 1991-01-09 | Amgen Inc. | Microbial expression of insulin-like growth factor |
| EP0189481A4 (en) * | 1984-07-13 | 1987-01-10 | Chiron Corp | Insulin-like Growth factor II. |
| US5070075A (en) * | 1986-01-07 | 1991-12-03 | Washington University | Human preproinsulin-like growth factor I |
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