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WO2013089076A1 - Gel prémoulé pour électrophorèse, son procédé de production et son procédé d'utilisation - Google Patents

Gel prémoulé pour électrophorèse, son procédé de production et son procédé d'utilisation Download PDF

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Publication number
WO2013089076A1
WO2013089076A1 PCT/JP2012/081997 JP2012081997W WO2013089076A1 WO 2013089076 A1 WO2013089076 A1 WO 2013089076A1 JP 2012081997 W JP2012081997 W JP 2012081997W WO 2013089076 A1 WO2013089076 A1 WO 2013089076A1
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WIPO (PCT)
Prior art keywords
gel
electrophoresis
hydroxymethyl
acid
tris
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PCT/JP2012/081997
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English (en)
Japanese (ja)
Inventor
由希子 峰岸
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Hymo Corp
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Hymo Corp
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Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N27/00—Investigating or analysing materials by the use of electric, electrochemical, or magnetic means
    • G01N27/26—Investigating or analysing materials by the use of electric, electrochemical, or magnetic means by investigating electrochemical variables; by using electrolysis or electrophoresis
    • G01N27/416—Systems
    • G01N27/447—Systems using electrophoresis
    • G01N27/44704—Details; Accessories
    • G01N27/44747—Composition of gel or of carrier mixture

Definitions

  • the present invention relates to a polyacrylamide precast gel for electrophoresis for biochemical drug analysis, a method for using the same, and a method for producing the same.
  • Polyacrylamide precast gels for electrophoresis are widely used as basic research tools in many fields such as biology, medicine, fisheries, and veterinary medicine for the purpose of detection and quantitative analysis of important substances constituting the living body such as proteins. ing.
  • polyacrylamide gel is an artificially synthesized substance, gels with different separation characteristics can be easily prepared by changing the formulation.
  • the use of precast gels that are mass-produced to have various separation characteristics in advance greatly reduces the labor of analysis, and contributes to production and quality control in this field because they are uniform and have good reproducibility.
  • it is expected that the storage stability is good.
  • Proteins are functionalized by more than 300 post-translational modifications in vivo, especially in mammals, where it is said that one third of proteins in the body are in a phosphorylated modified state, and the pathogenesis of various diseases In order to lead to early detection and treatment, the phosphorylation modification state of proteins has been investigated.
  • Non-Patent Document 2 a method using Tris or Tricine in an electrophoresis buffer proposed by Shagar et al. Is widely used. In the gel buffer solution in this method, Tris is neutralized with hydrochloric acid so that the pH is 8.45.
  • Patent Document 1 an example using the Remley method is proposed as an example.
  • Patent Document 4 As reported in Patent Document 3, Patent Document 4, and Patent Document 5, the present applicant has also conducted extensive research on quality improvement, production method, and use method of polyacrylamide gel for electrophoresis, and has solved the problem. There is a background.
  • the object of the present invention is to allow the use of Remley or Shagar's running buffer, which has a long-term stable protein separation and gel shape, and is widely used in analysis methods.
  • An object of the present invention is to provide a precast gel for electrophoresis which can be carried out and used for the purpose of analyzing the phosphorylation modification state of a protein.
  • the present invention includes 1) an aqueous acrylamide copolymer having a structure represented by the following formula (A) in at least a part of the structure and containing a buffer solution having the following compositions (1) and (2). It is related with the precast gel for electrophoresis characterized by being a gel. (1) Tris (hydroxymethyl) aminomethane and / or bis (2-hydroxyethyl) iminotris (hydroxymethyl) methane and one or more ampholytes. (2) pH is 6.0 to 6.8. Compound (A) In the formula, M 2+ is a transition metal ion.
  • the invention according to claim 2 is the precast gel for electrophoresis according to claim 1, wherein the one or more ampholytes in the gel buffer essentially comprise glycine and / or tricine.
  • the invention of claim 3 is characterized in that in one or more ampholytes, the range of the base dissociation constant of the ampholytes other than glycine and / or tricine is 6.6 to 9.6.
  • the ampholyte other than glycine and / or tricine is serine, threonine, phenylalanine, glutamic acid, tryptophan, methionine, alanine, valine, aspartic acid, N, N-bis (2-hydroxyethyl) glycine, tris (hydroxymethyl) methylaminopropanesulfonic acid, 2-aminoethylsulfonic acid, N, N-bis (2-hydroxyethyl) -2-aminoethanesulfonic acid, 3-N-morpholinopropanesulfonic acid, N-tris (hydroxymethyl) methyl-2-aminoethanesulfonic acid, N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid, N-2-hydroxyethylpiperazinepropane It is at least one selected from sulfonic acid, glycylglycine, tris (hydroxymethyl) methylamin
  • the invention of claim 5 is characterized in that the ampholyte other than glycine and / or tricine is contained in a range of 0.1 to 100 mol% with respect to glycine and / or tricine. Precast gel for electrophoresis.
  • the concentration of tris (hydroxymethyl) aminomethane and / or bis (2-hydroxyethyl) iminotris (hydroxymethyl) methane in the gel is 0.07 to 0.2 mol / L.
  • the invention of claim 7 includes acrylamide, the following compound (B), a crosslinking agent, tris (hydroxymethyl) aminomethane and / or bis (2-hydroxyethyl) iminotris (hydroxymethyl) methane, and one or more ampholytes.
  • a method for producing a precast gel for electrophoresis comprising polymerizing an aqueous mixture solution having a pH of 6.0 to 6.8.
  • Compound (B) In the formula, M 2+ is a transition metal ion.
  • the invention of claim 8 uses the precast gel for electrophoresis according to claims 1 to 6 and a buffer for electrophoresis containing tris (hydroxymethyl) aminomethane in which dodecyl sulfate is present and an ampholyte.
  • the resolution of the protein and the shape of the gel are stable for a long period of time, and it is possible to use the Remley or Shagar's running buffer, which is widely used for analysis, and the user can perform the analysis economically and efficiently.
  • the electrophoresis precast gel of the present invention comprises a separation medium for electrophoresis, a gel buffer, and a support for holding the separation medium.
  • the separation medium for electrophoresis of the present invention includes acrylamide, the following compound (B), a crosslinking agent, tris (hydroxymethyl) aminomethane and / or bis (2-hydroxyethyl) iminotris (hydroxymethyl) methane, and one or more kinds. It can be produced by polymerizing a mixed aqueous solution comprising an amphoteric electrolyte having a pH of 6.0 to 6.8.
  • M 2+ is a transition metal ion.
  • the compound (B) is preferably copolymerized in the range of 0.003 to 0.3% by mass with respect to acrylamide. If the amount is more than 0.3% by mass, the degree of polymerization is not sufficiently increased and is not suitable for use as a migration medium.
  • the transition metal ion of the compound (B) is preferably a divalent ion such as iron, manganese, copper, or zinc, and particularly preferably a divalent zinc ion.
  • Compound (B) may be mixed with acrylamide in a state where transition metal ions are coordinated, or a divalent transition metal compound may be added during polymerization to form a coordination structure in the copolymer.
  • As the transition metal compound zinc chloride, zinc acetate, zinc sulfate or the like can be used.
  • crosslinking agent general divinyl compounds such as N, N-methylenebisacrylamide and N, N-diallyltartaramide may be used.
  • the crosslinking agent is preferably copolymerized in the range of 0.5 to 7% by mass with respect to the total mass of acrylamide and compound (B). If it is 0.5 mass% or less, the gel becomes too soft and difficult to operate, and if it is 7 mass% or more, a clear separation pattern cannot be obtained.
  • the total of the acrylamide, the compound (B) and the crosslinking agent is 3 to 25% by mass.
  • the gel buffer contains tris (hydroxymethyl) aminomethane and / or bis (2-hydroxyethyl) iminotris (hydroxymethyl) methane and one or more ampholytes.
  • Glycine can be used as the ampholyte when using the Remley running buffer, and either glycine or tricine can be used when using the Shagar running buffer. Further, by combining glycine and / or tricine with other ampholytes, it is possible to expand the molecular weight range.
  • amphoteric electrolyte other than glycine or tricine preferably has a base dissociation constant in the range of 6.6 to 9.6.
  • ampholytes include glycine, tricine, serine, threonine, phenylalanine, glutamic acid, tryptophan, methionine, alanine, valine, aspartic acid, N, N-bis (2-hydroxyethyl) glycine, tris (hydroxymethyl) methylaminopropanesulfonic acid, 2-aminoethylsulfonic acid, N, N-bis (2-hydroxyethyl) -2-aminoethanesulfonic acid, 3-N-morpholinopropanesulfonic acid, N-tris (hydroxymethyl) methyl-2-aminoethanesulfonic acid, N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid, N-2-hydroxyethylpiperazinepropan
  • ampholytes are added to moderate the potential gradient in the gel so that the molecular weight cut-off range is suitable for protein separation and the separation pattern is clear.
  • electrophoresis is performed using Remley or Shagar's running buffer and a gel with a pH of 6.0 to 6.8, using a gel to which no ampholyte is added, the migration speed is high and the molecular weight range is extremely low. The result is a high molecular region, or the migration speed is slow and the separation pattern is unclear and unsuitable for separation.
  • the potential gradient in the gel changes more slowly than the case of glycine or tricine alone, because they move to the anode side in order from the lowest pKb.
  • a clear separation pattern can be obtained in a particularly low-molecular region of possible proteins.
  • the base dissociation constant pKb of the coexisting ampholyte is pKb ⁇ 6.6
  • the coexisting ampholyte becomes in an acid dissociation state in the gel, changes the pH of the gel buffer, and acts as a trailing ion. A band that should not be present is detected.
  • pKb> 9.6 since the base dissociation constant is higher than that of glycine, it does not contribute to the action of moderately changing the potential gradient in the gel.
  • the concentration of tris (hydroxymethyl) aminomethane and / or bis (2-hydroxyethyl) iminotris (hydroxymethyl) methane in the gel buffer is 0.07 mol / L to 0.2 mol / L, preferably 0.08 mol / L. L to 0.1 mol / L.
  • This range is a range in which the amount of leading ions in the gel necessary to have a migration time equivalent to that of a gel prepared using the Remley gel buffer can be contained.
  • the concentration of tris (hydroxymethyl) aminomethane in the gel is lower than 0.07 mol / L, the entire electrophoretic image becomes unclear and becomes unusable for protein separation analysis.
  • the Tris concentration in the gel is higher than 0.2 mol / L, the leading ion concentration in the gel is increased, the migration time is extended, and the analysis work efficiency is deteriorated.
  • the total concentration of glycine and / or tricine and the ampholyte coexisting with them is preferably 0.1 to 0.5 mol / L. Particularly preferred is 0.1 to 0.3 mol / L. If the total ampholyte concentration is less than 0.1 mol / L, the effect is small, and the electrophoretic image is unclear and the purpose of use cannot be achieved. You will not be able to get.
  • the amount of the coexisting ampholyte is preferably 0.1 to 100 mol% with respect to glycine and / or tricine.
  • the addition amount is lower than 0.1 mol%, it does not contribute to the action of slowing the change in the potential gradient in the gel, and when it is added more than 100 mol%, the separation pattern becomes unclear or should not be clear but originally. A band is detected.
  • the pH of the gel buffer is 6.0 to 6.8.
  • hydrolysis of the polyacrylamide gel tends to proceed, and the storage expiration date cannot be prolonged.
  • the pH is lower than 6.0, the stability as a polyacrylamide gel is good, but the electrophoretic image of the protein is unclear and unusable for practical use.
  • refrigerated storage lasts for 6 months, and at pH 6.3, the hydrolysis rate is remarkably reduced compared to pH 6.8 because it is close to the pH of acrylamide itself. As a result, the gel shape and electrophoretic image have not been changed for a long period of one year and are stable.
  • tris (hydroxymethyl) aminomethane and / or bis (2-hydroxyethyl) iminotris (hydroxymethyl) methane are neutralized with hydrochloric acid or acetic acid.
  • the precast gel of the present invention may contain a water-soluble polymer such as agarose, polyacrylamide, polyvinyl alcohol, polyvinyl pyrrolidone, polyethylene oxide, and polymethyl vinyl ether in order to give the gel elasticity and improve gel strength. .
  • a water-soluble polymer such as agarose, polyacrylamide, polyvinyl alcohol, polyvinyl pyrrolidone, polyethylene oxide, and polymethyl vinyl ether
  • the precast gel of the present invention is prepared by filling a glass or resin carrier with an aqueous solution containing acrylamide, the compound (B), a crosslinking agent and the gel buffer, and then subjecting the polymerization initiator and / or ultraviolet irradiation or ionization to the gel. It is produced by gelation with radicals generated by irradiation with sexual radiation.
  • a polymerization initiator a redox type that uses a peroxide such as ammonium persulfate (hereinafter abbreviated as APS) and a reducing agent such as N, N, N ′, N′tetramethylethylenediamine (hereinafter abbreviated as TEMED).
  • the peroxide and reducing agent are used in an amount of 0.05 to 5% (mass / volume) based on the total monomers.
  • the polymerization temperature is not particularly limited as long as it is a temperature at which the initiator functions, but is usually preferably in the range of 15 to 50 ° C.
  • the precast gel for electrophoresis of the present invention is used for separation according to the phosphorylation state of a protein using a buffer for electrophoresis containing tris (hydroxymethyl) aminomethane and an amphoteric electrolyte.
  • the composition of the electrophoresis buffer is preferably an electrophoresis buffer having a composition of Tris 0.025 mol / L, glycine 0.192 mol / L, and sodium dodecyl sulfate (hereinafter abbreviated as SDS) 0.1% by mass. .
  • SDS sodium dodecyl sulfate
  • an electrophoresis buffer having a composition of tris (hydroxymethyl) aminomethane 0.1 mol / L, tricine 0.1 mol / L, and SDS 0.1% by mass.
  • This composition is generally used as a buffer for electrophoresis of a sugar, particularly for the separation of low molecular weight proteins by gel electrophoresis.
  • Preparation method of precast gel for electrophoresis Silicon seal to prevent leakage of 1 mm spacer and monomer liquid between a rectangular glass plate with a width of 12 cm and a length of 10 cm and a glass plate of the same size with a concave cut at the top. Assemble the glass plate.
  • Acrylamide concentration 12% by mass (acrylamide + crosslinking agent, total concentration)
  • Compound (B) 0.03% by mass of acrylamide (using zinc as transition metal), 3% by mass of N, N-methylenebisacrylamide (vs.
  • a monomer containing an acrylamide concentration of 5% by mass (acrylamide + crosslinking agent, total concentration), N, N-methylenebisacrylamide 3% by mass (based on acrylamide concentration), and a gel buffer having the composition described in Table 1.
  • the solution was injected onto the separation layer and polymerized at 25 ° C. to obtain a concentrated layer of polyacrylamide gel for electrophoresis. .
  • Electrophoresis test method Electrophoresis was carried out using an electrophoresis buffer of Remley formulation of Tris 0.025 mol / L, glycine 0.192 mol / L, and SDS 0.1% by mass. ⁇ -casein and dephosphorylated ⁇ -casein were electrophoresed as protein samples. Dephosphorylated ⁇ -casein was dephosphorylated by adding alkaline phosphatase (manufactured by Nippon Gene) to the ⁇ -casein solution and allowing it to stand overnight. Electrophoresis was performed at a constant current of 20 mA, and energization was stopped when the migration terminal was 10 mm from the bottom.
  • alkaline phosphatase manufactured by Nippon Gene
  • Example 2 A precast gel prepared by the same method as in Example-1 was stored for 8 months under refrigeration, and then a migration test was performed in the same manner as in Example-1. The results are shown in Example 2 in Table 2-1.
  • Example 3 An electrophoresis test was performed in the same manner as in Example 1 except that a precast gel was prepared using the gel buffer of Example 3 in Table 1. The results are shown in Example 3 in Table 2-1.
  • Example 4 The migration test was performed in the same manner as in Example-1, except that the acrylamide concentration was changed to 7.5% (acrylamide + crosslinking agent vs. total concentration) and the precast gel was prepared using the gel buffer of Example-4 in Table 1. Carried out. The results are shown in Example 4 in Table 2-1.
  • a precast gel was prepared in the same manner as in Example 1 except that the gel buffer of Example-5 in Table 1 was used. Electrophoresis was performed using a running buffer of a Shagar formulation of Tris 0.1 mol / L, Tricine 0.1 mol / L, SDS 0.1 mass%. The protein sample and detection method were the same as in Example 1. The results are shown in Example-5 in Table 2-1.
  • Comparative Example 1 (Comparative Example 1) Performed except that a precast gel was prepared using 0.375 mol / L Tris-hydrochloric acid gel buffer pH 8.8 for the separation layer and 0.125 mol / L Tris-hydrochloric acid gel buffer pH 6.8 for the concentration layer. A migration test was performed as in Example-1. The results are shown in Comparative Example-1 in Table 2-2.
  • Comparative Example-2 A precast gel prepared in the same manner as in Comparative Example-1 was stored for 6 months under refrigeration, and then a migration test was performed in the same manner as in Example-1. The results are shown in Comparative Example-2 in Table 2-2.
  • Comparative Example-4 A precast gel was prepared and a migration test was conducted in the same manner as in Example 1 except that the compound (B) was not added. The results are shown in Comparative Example-4 in Table 2-2.
  • phosphorylated ⁇ -casein and dephosphorylated ⁇ -casein are both clear bands, and a clear mobility difference can be obtained.
  • the precast gel was able to separate proteins according to their phosphorylation state using Remley or Shagar's running buffer.
  • the precast gel for electrophoresis of the present invention can clearly separate the phosphorylated state of the protein and has the long-term stability required for the precast gel.
  • the separation ability of the protein and the shape of the gel are stable for a long period of time, and it is possible to use the Remley or Shagar electrophoresis buffer which is widely used for the analysis method. In particular, it is possible to analyze the phosphorylation modification state of a protein, and its industrial applicability is very large.

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Abstract

La présente invention concerne un gel prémoulé pour électrophorèse, le gel pouvant être utilisé pour analyser l'état de modification par phosphorylation d'une protéine, avec les solutions tampons d'électrophorèse de Laemmli ou de Schagger qui sont utilisées dans les procédés d'analyse les plus répandus, et qui peut être utilisé de manière économique et efficace par un utilisateur. Le gel prémoulé pour électrophorèse selon l'invention est un gel aqueux de copolymère d'acrylamide qui possède une structure spécifique dans au moins une partie de sa structure et qui contient une solution tampon ayant la composition (1) et la propriété (2) : (1) le tris(hydroxyméthyl)aminométhane et/ou le bis(2-hydroxyéthyl)iminotris(hydroxyméthyl)méthane, et au moins un électrolyte amphotère ; et (2) une valeur de pH allant de 6,0 à 6,8.
PCT/JP2012/081997 2011-12-16 2012-12-11 Gel prémoulé pour électrophorèse, son procédé de production et son procédé d'utilisation Ceased WO2013089076A1 (fr)

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JP2011-275630 2011-12-16
JP2011275630A JP5967751B2 (ja) 2011-12-16 2011-12-16 電気泳動用プレキャストゲル、その製造方法および使用方法

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Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP3362786B1 (fr) * 2015-10-14 2024-02-28 Life Technologies Corporation Gel d'électrophorèse ayant une durée de conservation prolongée et une efficacité élevée

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2016002282A1 (fr) * 2014-07-04 2016-01-07 アトー株式会社 Solution tampon de gel pour électrophorèse et gel de polyacrylamide pour électrophorèse

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2001159621A (ja) * 1999-12-02 2001-06-12 Hymo Corp 電気泳動用ポリアクリルアミドプレキャストゲル、その製造方法及びその使用方法
WO2007015312A1 (fr) * 2005-08-01 2007-02-08 Nard Institute, Ltd. Gel de polyacrylamide pour électrophorèse, procédé d’électrophorèse en gel de polyacrylamide utilisant celui-ci, procédé de production de celui-ci et composé acrylamide

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2002277438A (ja) * 2001-03-22 2002-09-25 Hymo Corp 電気泳動ゲル、その製法及びその使用法

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2001159621A (ja) * 1999-12-02 2001-06-12 Hymo Corp 電気泳動用ポリアクリルアミドプレキャストゲル、その製造方法及びその使用方法
WO2007015312A1 (fr) * 2005-08-01 2007-02-08 Nard Institute, Ltd. Gel de polyacrylamide pour électrophorèse, procédé d’électrophorèse en gel de polyacrylamide utilisant celui-ci, procédé de production de celui-ci et composé acrylamide

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP3362786B1 (fr) * 2015-10-14 2024-02-28 Life Technologies Corporation Gel d'électrophorèse ayant une durée de conservation prolongée et une efficacité élevée

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