• Journal of Pharmacopuncture
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• v.9 no.2
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• pp.105-111
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• 2006

Objectives : This study was conducted to carry out Purification of Melittin and other peptide components from Bee Venom using gel filtration chromatography and propionic acid/urea polyacrylamide gel electrophoresis Methods : Melittin and other peptide components were separated from bee venom by using gel filtration chromatography on Sephadex G-50 column in 0.05M ammonium acetate buffer. Results : Melittin and other peptide components were separated from bee venom by using gel filtration chromatography on Sephadex G-50 column in 0.05M ammonium acetate buffer. The fractions obtained from gel filtration chromatography was analyzed by using SDS-PAGE and propionic acid/urea polyacrylamide gel electrophoresis. The melittin obtained from the gel filtration contained residual amount of phospholipase $A_2$ and a protein with molecular weight of 6,000. The contaminating proteins were removed by the second gel filtration chromatography. Conclusion : Gel filtration chromatography and propionic acid/urea polyacrylamide gel electrophoresis are useful to separate peptide components including melittin from bee venom.

• Korean Journal of Microbiology
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• v.28 no.3
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• pp.278-282
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• 1990

Diffusion and partition of progesterone into the polyacrylamide gel was examined. Diffusion coefficient of progesterone decreased down to an asymptotic value as the concentration of the organic solvents in the diffusing medium increased. However the partition coefficient diminished steadily. Crosslinking density in the gel didn't affected the diffusion coefficient considerably but lowered the partition coefficient due to the contraction of pore volume of the gel. Progesterone showed higher diffusion coefficient as well as partition coefficient in the polyurethane than in the polyacrylamide gel, which seems to be ascribed to the difference in hydrophobicity, pore volume and pore size of the polymer matrix.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.30 no.4
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• pp.405-411
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• 1985

The buffer soluble proteins were extracted from six cultivars of barley grains and analyzed by various electrophoresis; 7.5% polyacrylamide slab gel, 2-30% polyacrylamide porosity gradient tube gel, isoelectric focusing (pH4-9) and starch gel electrophoresis. The proteins, esterase, acid phosphatase, malate dehydrogenase, glutamate dehydrogenase and leucine aminopeptidase were investigated to find out the best method to differentiate barley cultivars. The result were that protein and esterase bands in 2-30% polyacrylamide porosity gradient tube gel electrophoresis and protein bands in 7.5% polyacrylamide slab gel electrophoresis showed typical varietal differences. Therefore, those methods were suitable for differentiation of barley cultivars. It was difficult to differentiate the cultivars by the other methodes and patterns of the other enzymes.

• Korean Journal of Food Science and Technology
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• v.17 no.1
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• pp.1-4
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• 1985

For the systematic investigation of biochemical characteristics of Korean ginseng protein by years, protein fractions were analyzed by the techniques of polyacrylamide gel electrophoresis, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration, while the amino acid composition was studied by amino acid autoanalyzer. Results of polyacrylamide gel electrophoresis and SDS-PAGE showed a few difference in pattern and number of bands depending on the age of the root. However, the number of bands obtained from polyacrylamide gel electrophoresis and SDS-PAGE was 8 and 7 to 11, respectively. When water extracted proteins were fractionated by Sephadex G-200, the main peak among 2 peaks was collected and lyophillized. Its mol. wt. was extimated to be 43,000 by the SDS-PAGE method. In amino acid composition of water extracted protein and main fraction of gel filtration, arginine content was the highest, 47.17% in water extracted protein and 57.36% in main fraction followed by glutamic acid and asparatic acid. On the contrary, cystine and methionine contents were very low in both cases.

• Microbiology and Biotechnology Letters
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• v.9 no.4
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• pp.185-190
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• 1981

1. $\alpha$-amylase from B. circulans F-2 was purified with specific activity 55.0 u/mg. protein (about 23 times of the original specific activity) and the yield of 25.5%, by means of corn starch absorption, salting out with ammonium sulfate (80% saturation), gel filtration on Bio-Gel P-100 and DE-32 column chromatography. 2 The purified enzyme showed two closely migrated protin bands on polyacrylamide disc gel electrophoresis, both of which have amylase activity judging from the activity staining of the gel. On SDS-polyacrylamide disc gel electrophoresis, however, the purified enzyme showed a single band suggesting that those two bands are the charge isomers of an amlyase having the slightly different charge. 3. Plot of log mobility of two bands versus polyacrylamide gel concentration according to Hedrick and Smith gave the parallel lines indicating them to be charge isomers. 4. To confirm the action pattern of two enzyme protein bands, each band was separated and was eluted from the gel and eluates were incubated with soluble starch. Oligosaccharide pattern produced by each eluate was examined by paper chromatography. The eluates of two bands showed the same action pattern. 5. The maltohexaose was the only hydrolysis product of soluble starch in the early stage of hydrolysis.

• Korean Journal of Microbiology
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• v.27 no.4
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• pp.436-438
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• 1989

We propose a method for rapid evaluation and permanent record of sodium dodecyl sulfate polyacrylamide gel electrophoretic runs. This method is based on the photocopy process, rather than on photography and requires no extensive or expensive investment. Comparison of a print obtained through this method and a 35mm photography indicated, on a balanced gel, equal sensitivity.

• Asian Journal of Turfgrass Science
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• v.5 no.1
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• pp.11-22
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• 1991

This experiment was executed to investigate the possibility of the application of taxonomic method through the isoelectric focusing with polyacrylamide gel and sodium dodecyl sulfate-polyacrylamide gel electrophoresis with seeds in the identification of turfgrasses. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to investigate the pattern of seed proteins which were extracted from 18 cultivars of cool season turfgrass and 4 cultivars of warm season turfgrass. The isoelectric focusing with polyacrylarnide gel was used to investigate the activity of the three isozymes of esterase, peroxidase and phosphoglucose isomerase which were extracted from 18 cultivars of cool season turfgrass and 4 cultivars of warm season turfgrass. The results were summarized as follows. 1. The difference of the patterns of seed proteins was observed with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The identification of intra-genus was easily detected. 2. The three isozymes of esterase, peroxidase and phosphoglucose isomerase were investigated through isoelectric focusing with polyacrylamide gel. As a result, esterase was most effective among three isozymes in the identification of turfgrass cultivars 3. In the past cultivar identification was primarily based on visual morphological characters, but there was a lot of difficulty. If we should use electrophoresis, we will be able to identifvturfgrass cultivars more effectively.

• Korean Journal of Microbiology
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• v.26 no.4
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• pp.324-331
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• 1988

Ascorbate oxidizing enzyme from the crude extract of Pleurotus ostreatus was purified by ammonium sulfate precipitation, preparative polyacrylamide gel electrophoresis, DEAE Sepharose CL-6B ion exchange chromatography and Sephadex G-150 gel filtration chromatography. The molecular weight of the enzyme estimated by Sephadex G-150 gel filtration chromatography was 140,000 and that of its subunit by SDS-polyacrylamide gel electrophoresis 66,000. The optimum pH for the maximum activity of the enzyme was 5.2 and the isoelectric point of the enzyme was 6.0 Km values for L-ascorbic acid and D-isoascorbic acid were both 2.2.$\mu$M, which indicates that the enzyme has the asme affinity towards both substrates.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.50 no.spc1
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• pp.228-230
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• 2005

The denature polyacrylamide gel stain silver nitrate is used for routine nucleic acid detection. More sensitive stains, such as Vistra Green, SYBR Green are available to address a broad range of DNA applications requiring lower detection limits in polyacrylamide gel formats. Gel Scanners, laser-scanning instruments, provide sensitive fluorescence detection of DNA gel stains. We established one step fluorescent impregnation enhanced sensitivity with simple, rapid and low cost. We have applied this fluorescent staining procedure for the routine analysis of DNA profiles generated by SSR amplification.

• Journal of the Korean Wood Science and Technology
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• v.18 no.2
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• pp.36-48
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• 1990

This experiment was carried out to improve the quality of high absorbent polymer which has excellent absorptivity and water retention compared to pulp and absorption sheet, through absorption characteristics-absorptive power, water retention, absorption rate, gel strength, pH, particle size, and moisture content. - of six polymers, namely, anionic polyacrylamide, cationic polyacrylamide, polyacrylic, acid polyvinyle alcohol 500, and 1500, and a-cellulose. and to examine the possibility of substitution of amide groups for carboxyl group and/or hydroxyl group which were commercial high absorbent polymer by comparing the absorption characteristics of the polymers. Polyacrylamide has high absorptive power and water retention, but has low gel strength and poor absorption rate. The rest of polymers were similiar to ${\alpha}$-cellulose in every respect. Thus, polyacrylamides could be replaced with polyacrylic acid and polyvinyl alcohol which are presently a high absorbent polymers. In comparing the absorption characteristics and the absorptive power of the polymers-anionic polyacrylamide, cationic polyacrylamide, polyacrylic acid, polyvinyle alcohol. a-cellulose-the absorptive power was in inverse proportion to the gel strength and absorption rates, affected by the particle size and pH change.