CN114791458A - Gel for separating protein through electrophoresis, buffer solution used in cooperation with gel and kit of gel - Google Patents
Gel for separating protein through electrophoresis, buffer solution used in cooperation with gel and kit of gel Download PDFInfo
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- CN114791458A CN114791458A CN202210440812.2A CN202210440812A CN114791458A CN 114791458 A CN114791458 A CN 114791458A CN 202210440812 A CN202210440812 A CN 202210440812A CN 114791458 A CN114791458 A CN 114791458A
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- 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
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- 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
- G01N27/44756—Apparatus specially adapted therefor
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- 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
- G01N27/44756—Apparatus specially adapted therefor
- G01N27/44773—Multi-stage electrophoresis, e.g. two-dimensional electrophoresis
- G01N27/44778—Multi-stage electrophoresis, e.g. two-dimensional electrophoresis on a common gel carrier, i.e. 2D gel electrophoresis
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Abstract
The invention belongs to the field of protein electrophoresis reagents, and discloses gel for separating proteins through electrophoresis, a buffer solution matched with the gel and a kit of the buffer solution. Comprises gel containing gel buffer, gel system stabilizer, protein solubilizer, acrylamide, gel electrophoresis buffer containing 2, 2-bis (dimethylol aniline) or tris (hydroxymethyl) aminomethane, 3-morpholine propanesulfonic acid (MOPS) or 2-N-morpholine alkane sulfonic acid (MES), sodium dodecyl sulfate and EDTA, and gel electrophoresis kit containing the gel and the gel electrophoresis buffer. The invention can reduce the dosage of the main buffer to 100mM-150mM, and the glutamic acid is added in the invention, which can prevent the accumulation of hydrogen ions at the bottom of the gel, thereby avoiding the situation that the partial pH of the gel is lower than 2 and the protein can not migrate.
Description
Technical Field
The invention belongs to the field of protein electrophoresis reagents, and discloses gel for separating proteins by electrophoresis, buffer solution matched with the gel and a kit of the gel.
Background
Polyacrylamide gel electrophoresis is mainly used for separating proteins and nucleic acids, is widely used in the fields related to biochemistry such as biology, medicine and the like, and can prepare polyacrylamide gels with different pore diameters by changing the concentration of acrylamide before polymerization. In 1970, laemmli created sodium dodecyl sulfate-containing denaturing polyacrylamide gels (SDS-PAGE), abbreviated as laemmli system gels, and this technique was widely used for protein analysis.
The traditional laemmli system uses tris as a buffer to control the pH of the gel, with the pH of the underlying gel being 8.8. The laemmli system gel has good separation effect and strip definition, but due to the alkaline environment in the gel, the polymerized polyacrylamide is easy to hydrolyze, the migration of protein in the electrophoresis process is disturbed, and the strip of the protein is blurred.
When the pH value of the gel is adjusted to be slightly acidic, the stability of the polyacrylamide gel is greatly improved, the gel can be prepared in advance, the operation time of a protein electrophoresis experiment is greatly saved, and the stability of a protein electrophoresis result is also improved due to batch preparation.
Because the core of the method is to control the pH value of the buffer in a slightly acidic environment, the currently used buffer mainly comprises two types of bis (2-hydroxymethyl) amino-tris (hydroxymethyl) methane and tris (hydroxymethyl) aminomethane. The electrophoresis is greatly influenced by the types of the trailing ions in the electrophoresis, the electrophoresis is mainly divided into the traditional glycine and a zwitterionic buffer (Good's buffer), the Good's buffer mainly comprises three types of MOPS, MES and HEPES which are used as the trailing ions in the electrophoresis, and when the three types of the buffer are used, compared with a laemmli system, the electrophoresis migration speed is higher, the time can be saved, the probability of protein modification in the electrophoresis process is lower, but the migration position of the protein in the gel of the system is greatly different from that of the traditional laemmli system in the separation process, and the price of raw materials is very high.
In electrophoresis, hydrogen ions are accumulated in an anode region along with the electrophoresis, the bis (2-hydroxymethyl) amino-tris (hydroxymethyl) methane and the tris (hydroxymethyl) aminomethane in the two buffering agents have the effect of ensuring the stability of the pH value in the gel, and if the buffering capacity is not enough, the hydrogen ions cannot be absorbed, so that the pH value of the bottom of the gel, which is close to the anode region, is greatly reduced, and the protein cannot migrate at the lower part of the gel. The existing methods cannot reduce the cost by reducing the concentration of the buffer.
When electrophoresis is performed in a prefabricated gel system, the actual loading capacity during electrophoresis is lower than that of the traditional method due to the low pH value compared with the traditional laemmli system, and when proteins are separated through electrophoresis, the migration of the proteins during electrophoresis cannot be influenced by particles sometimes.
Disclosure of Invention
In view of the above situation, the invention discloses a gel for separating proteins by electrophoresis, a buffer solution matched with the gel and a kit thereof.
The technical scheme of the invention is as follows:
a gel for separating proteins by electrophoresis comprising the following components:
gel buffer: 2, 2-bis-dimethylolaniline or tris (hydroxymethyl) aminomethane;
gel system stabilizer: one or more of glutamic acid, citric acid, malic acid and succinic acid;
protein solubilizer: dimethylformamide;
acrylamide: n, N-methylene bisacrylamide.
Further, the gel for separating proteins by electrophoresis is prepared by a catalyst: ammonium persulfate and TEMED.
Further, the gel buffer: the concentration of the 2, 2-bis-dimethylolaniline or tris (hydroxymethyl) aminomethane component is 100-400mM, preferably 100-150 mM.
Furthermore, the gel system stabilizer is glutamic acid, citric acid, malic acid and succinic acid in any proportion, and the component concentration is 1-50 mM.
Further, the ratio of acrylamide: n, N-methylene bisacrylamide, and the component concentration is 700mM-3000 mM.
Further, the protein solubilizing agent: the concentration of the dimethylformamide component is 1mM-100 mM.
Further, the pH value of the gel is 6.4-6.6.
The gel electrophoresis buffer matched with the protein gel separated by electrophoresis comprises the following components:
1.2, 2-bis (hydroxymethyl) aniline or tris (hydroxymethyl) aminomethane, with the component concentration of 10-100 mM;
2.3-morpholinopropanesulfonic acid (MOPS) or 2-N-morpholinoalkanesulfonic acid (MES) in a concentration of 10 to 100 mM;
3. sodium dodecyl sulfate with the component concentration of 1-5 mM;
EDTA with the component concentration of 0.1-3 mM.
Further, the gel electrophoresis kit comprises the gel and the gel electrophoresis buffer solution which are mixed according to any proportion.
Compared with the prior art, the invention has the following beneficial effects:
because the pH value of the gel needs to be controlled by a buffering agent, the concentration needs to be higher than a certain concentration, the acidic amino acid (glutamic acid) is added into the existing formula, and the glutamic acid improves the buffering capacity of the gel in an acidic region and prevents acidification; meanwhile, the stability of the gel can be improved due to the addition of glutamic acid; the buffer interval of the glutamic acid is about pH 3, the added glutamic acid can be combined with hydrogen ions through carboxyl and amino to prevent the hydrogen ions from being accumulated, and meanwhile, the amido bond of the polyacrylamide is hydrolyzed into carboxyl, so the added glutamic acid can also play a reverse inhibiting role. Because the pH value of the gel is neutral or influenced by the trailing ions, the electrophoretic separation protein capacity is low, and the tolerance to a sample with insoluble particles is poor, the dimethylformamide is added in the invention, the solubility of the sample is improved, the protein capacity is improved, and the gel can be prevented from being blocked by the insoluble particles. Dimethylformamide is a widely used excellent solvent, can be used as a good solvent for various high molecular polymers, and can be used as a protein solubilizer in polyacrylamide gel by analogy to increase the solubility of protein in the migration process.
Compared with the prior art, the method can reduce the dosage of the main buffer to 100mM-150mM, and the glutamic acid is added in the method, so that accumulation of hydrogen ions at the bottom of the gel can be prevented, and the situation that the protein cannot migrate because the local pH of the gel is lower than 2 is avoided (the intuitive expression of hydrogen ion accumulation is that bromophenol blue turns yellow, cannot move and deforms).
Meanwhile, the gel provided by the invention can increase the solubility of protein, avoid excessive insoluble particles in a sample and enable an electrophoresis band to be straighter.
Drawings
FIG. 1 is an electrophoretogram in example 1;
FIG. 2 is an electrophoretogram in example 2;
FIG. 3 is an electrophoretogram in example 3;
FIG. 4 is a linear plot of the separation of formulation one (on-day formulation) of example 4, where the abscissa is the logarithmic value of the protein migration molecular weight based on 10 and the ordinate is the distance of the upper edge of the migration band from the lower edge of bromophenol blue;
FIG. 5 is a linear plot of the separation of formulation one (twelve days at 37 ℃ C. after formulation) of example 4, where the abscissa is the logarithmic value of the protein migration molecular weight to base 10 and the ordinate is the distance of the upper edge of the migration band from the lower edge bromophenol blue;
FIG. 6 is a linear plot of the separation for formulation two (on-day formulation) of example 4, where the abscissa is the logarithmic value of the protein migration molecular weight based on 10 and the ordinate is the distance of the upper edge of the migration band from the lower edge of bromophenol blue;
FIG. 7 is a linear plot of the separation of formula two (twelve days at 37 ℃ C. after formulation) of example 4, where the abscissa is the logarithmic value of the protein migration molecular weight to the base 10 and the ordinate is the distance of the upper edge of the migration band from the lower edge bromophenol blue;
FIG. 8 is a linear plot of the separation of formula three (on the day) in example 4, where the abscissa is the logarithmic value of the protein migration molecular weight based on 10 and the ordinate is the distance of the upper edge of the migration band from the lower edge of bromophenol blue;
FIG. 9 is a linear plot of the separation of formulation three (twelve days at 37 ℃ C. after formulation) of example 4, plotted on the abscissa the log value of the protein migration molecular weight to base 10 and on the ordinate the distance of the upper edge of the migration band from the lower edge bromophenol blue.
Detailed Description
The test methods used in the following examples are all conventional methods unless otherwise specified.
Materials, reagents and the like used in the following examples are commercially available unless otherwise specified.
Example 1
This example compares polyacrylamide gels of the present invention with glutamic acid and dimethylformamide added thereto with polyacrylamide gels (other patent reported formulations, or literature published formulations) that are not within the scope of the present invention. The separation was performed the next day the gel was prepared.
An aqueous solution having a polyacrylamide concentration of 12% (T12%, C2.6%, C N, mass of N methylene bisacrylamide/mass of acrylamide + N, mass of N methylene bisacrylamide, concentration of N, N methylene bisacrylamide 1688mM) was prepared using a glass plate or a plastic plate. The gel making solution contains a density agent, namely 8% of glycerol, the pH value is adjusted to 6.4-6.6 by using hydrochloric acid, and ammonium persulfate and TEMED are used as catalysts to catalyze N, N-methylene-bisacrylamide to polymerize and crosslink to form three-dimensional reticular polyacrylamide gel. The control solution is prepared into polyacrylamide gel with the same concentration (the catalytic part is a conventional method or a technique known in the art, and the invention is not particularly limited in this regard). The specific formulation is shown in table 1 below.
Table 1: formulation of example 1
The test electrophoresis buffer used was prepared with 50mM Tris-Tris, 50mM 3-morpholinopropanesulfonic acid, 0.1% SDS and EDTA using Mini-Protean type electrophoresis cell. The samples isolated were samples of different concentrations prepared from mouse liver tissue. As shown in fig. 1, when the obtained electrophorogram is compared, the band shape of the patent formula (fig. 1, left) is flatter at a high concentration, and insoluble particles accumulated at an excessively high concentration do not appear in the band.
Example 2
This example compares polyacrylamide gels of the present invention with glutamic acid and dimethylformamide added thereto with polyacrylamide gels (other patent reported formulations, or literature published formulations) not within the scope of the present invention, and tests were performed after 12 days of standing at 37 degrees celsius after formulation.
An aqueous solution of 12% polyacrylamide concentration (T12%, C2.6%, N-methylene bisacrylamide concentration 1688mM) was prepared using a glass plate or a plastic plate. The glue making solution contains a density agent of 8% of glycerol, the pH value is adjusted to 6.4-6.6 by using hydrochloric acid, and ammonium persulfate and TEMED are used as catalysts to catalyze N, N-methylene bisacrylamide to polymerize and crosslink to form three-dimensional reticular polyacrylamide gel. The control solution is prepared into polyacrylamide gel with the same concentration (the catalytic part is a conventional method or a technique known in the art, and the invention is not particularly limited in this regard). The specific formulation is shown in table 2 below:
table 2: formulation of example 2
The test electrophoresis buffer used was prepared with 50mM Tris-Tris, 50mM 3-morpholinopropanesulfonic acid, 0.1% SDS and EDTA using Mini-Protean type electrophoresis cell. The samples isolated were samples of different concentrations prepared from mouse liver tissue. Comparing the electrophorograms obtained according to fig. 2, the patented formulation (right of fig. 2) was electrophoresed after a long time of standing until the bottom of the gel did not yellow (showing that the color of bromofinland turned yellow), while the control gel (left of fig. 2) turned yellow at the bottom, resulting in a bottom result that was not obtained.
Example 3
This example compares the polyacrylamide gels of glutamic acid and dimethylformamide with the optional stabilizer malic acid added in accordance with the invention, after 12 days at 37 ℃ after formulation, with the same formulation gels formulated on the same day.
An aqueous solution of 12% polyacrylamide concentration (T12%, C2.6%, N methylenebisacrylamide concentration 1688mM) was prepared using a glass plate or a plastic plate. The gel making solution contains a density agent, namely 8% of glycerol, the pH value is adjusted to 6.4-6.6 by using hydrochloric acid, and ammonium persulfate and TEMED are used as catalysts to catalyze N, N-methylene-bisacrylamide to polymerize and crosslink to form three-dimensional reticular polyacrylamide gel. The control solution is prepared as polyacrylamide gel of the same concentration (the catalytic portion is conventional or well known in the art, and the invention is not particularly limited in this regard). The specific formulation is shown in table 3:
table 3: formulation of example 3
The test electrophoresis buffer used was prepared with 50mM Tris-Tris, 50mM 3-morpholinopropanesulfonic acid, 0.1% SDS and EDTA using Mini-Protean type electrophoresis cell. The separated samples are samples with different concentrations prepared by mouse liver tissues, pre-stained markers, non-pre-stained markers and escherichia coli lysates. The electrophorograms obtained were compared as shown in FIG. 3, and in FIG. 3, the gel was prepared the same day on the left side, and after 12 days at 37 ℃ on the right side, there was no significant change except for a slight dispersion of some bands.
Example 4
This example is also a thermally accelerated test to investigate the effect of using different combinations and concentrations of buffers and stabilizers on polyacrylamide gel stability, especially strip mobility, within the scope of the invention. An aqueous solution of 10% polyacrylamide (T12%, C2.6%) was prepared using a glass or plastic plate according to the gel formulation in the table below, with a concentration of 1407mM for N, N methylenebisacrylamide. The glue making solution contains a density agent of 8% of glycerol, the pH value is adjusted to 6.4-6.6 by using hydrochloric acid, and ammonium persulfate and TEMED are used as catalysts to catalyze N, N-methylene bisacrylamide to polymerize and crosslink to form three-dimensional reticular polyacrylamide gel. The control solution is prepared into polyacrylamide gel with the same concentration (the catalytic part is a conventional method or a technique known in the art, and the invention is not particularly limited in this regard).
| Name of the formulation | Discriminating component |
| Formulation A | 200Mm Bis-Tris; 30Mm glutamic acid; 10mM dimethylformylAmines as pesticides |
| Formulation B | 300Mm Tris; 30Mm glutamic acid; 10mM dimethylformamide |
| Formulation C | 300Mm Tris; 30Mm glutamic acid; 50mM dimethylformamide |
The test electrophoresis buffer used was prepared with 50mM Tris-Tris, 50mM 3-morpholinopropanesulfonic acid, 0.1% SDS and EDTA using Mini-Protean type electrophoresis cell. The separated sample is a non-prestained protein molecular weight standard, the formula is placed for 12 days at 37 ℃ after preparation, gel is prepared on the day of use, migration positions of the non-prestained protein molecular weight standard in glue with different formulas and glue with different storage time are compared, and a protein molecular weight migration rate formula is as follows: lgMr ═ -b × mR + K. Because the gel separation range is linear, but one concentration is only linear in a certain protein molecular weight separation range, for example, 10% concentration gel is linear in the protein molecular weight range of 40-70 KDa. The results are shown in FIGS. 4-9, where the migration positions of the protein marker are substantially consistent with the distribution ratio and the storage time of different components.
It will be evident to those skilled in the art that the invention is not limited to the details of the foregoing illustrative embodiments, and that the present invention may be embodied in other specific forms without departing from the spirit or essential attributes thereof. The present embodiments are therefore to be considered in all respects as illustrative and not restrictive, the scope of the invention being indicated by the appended claims rather than by the foregoing description, and all changes which come within the meaning and range of equivalency of the claims are therefore intended to be embraced therein.
Furthermore, it should be understood that although the present specification describes embodiments, not every embodiment includes only a single embodiment, and such description is for clarity purposes only, and it is to be understood that all embodiments may be combined as appropriate by one of ordinary skill in the art to form other embodiments as will be apparent to those of skill in the art from the description herein.
Claims (10)
1. A gel for separating proteins by electrophoresis, the gel comprising:
gel buffer: 2, 2-bis-dimethylolaniline or tris (hydroxymethyl) aminomethane;
gel system stabilizer: one or more of glutamic acid, citric acid, malic acid and succinic acid;
protein solubilizer: dimethylformamide;
acrylamide: n, N-methylene bisacrylamide.
2. The gel for separating proteins by electrophoresis as claimed in claim 1, wherein the gel is prepared by contacting the protein with a catalyst: ammonium persulfate and TEMED.
3. The gel for separating proteins by electrophoresis as recited in claim 1, wherein said gel buffer: the component concentration of 2, 2-bis-dimethylolaniline or tris (hydroxymethyl) aminomethane was 100-400 mM.
4. The gel for separating proteins by electrophoresis as claimed in claim 1, wherein the gel system stabilizer is glutamic acid, citric acid, malic acid, succinic acid at any ratio, and the concentration of the components of the gel system stabilizer is 1-50 mM.
5. The gel for separating proteins by electrophoresis as claimed in claim 1, wherein the protein solubilizing agent: the concentration of the component dimethyl formamide is 1mM-100 mM.
6. The gel for separating proteins by electrophoresis as claimed in claim 1, wherein the acrylamide; the component concentration of the N, N-methylene bisacrylamide is 700mM-3000 mM.
7. The gel for separating proteins by electrophoresis as claimed in claim 1, wherein the pH of the gel is 6.4-6.6.
8. A gel electrophoresis buffer for use with a gel for separating proteins by electrophoresis according to any one of claims 1 to 7 comprising:
a first step of reacting 2, 2-bis-dimethylolaniline or tris (hydroxymethyl) aminomethane;
3-morpholinopropanesulfonic acid or 2-N-morpholinoalkanesulfonic acid;
③ sodium dodecyl sulfate;
④EDTA。
9. the gel electrophoresis buffer of claim 8 wherein the concentration of the 2, 2-bis-dimethylolaniline or tris is 10-100mM, the concentration of the 3-morpholinopropanesulfonic acid or 2-N-morpholinoalkanesulfonic acid is 10-100mM, the concentration of the sodium dodecylsulfate is 1-5mM, and the concentration of the EDTA is 0.1-3 mM.
10. A kit for gel electrophoresis comprising the gel for separating proteins by electrophoresis according to any one of claims 1 to 7 and the gel electrophoresis buffer according to claim 7 mixed at an arbitrary ratio.
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