• BMB Reports
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• v.41 no.3
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• pp.254-258
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• 2008

Lipase was purified from squid (Todarodes pacificus) liver in an attempt to investigate the possibility of applying the enzyme for biotechnological applications. Crude extract of squid liver was initially fractionated by the batch type ion exchange chromatography. The fraction containing lipase activity was further purified with an octyl-Sepharose column. Finally, lipase was purified by eluting active protein from a non-dissociating polyacrylamide gel after zymographic analysis. Molecular weight of the purified enzyme was determined to be 27 kDa by SDS-polyacrylamide gel electrophoresis. The enzyme showed the highest activity at a temperature range of $35-40^{\circ}C$ and at pH 8.0. The activity was almost completely inhibited at 1 mM concentration of $Hg^{2+}$ or $Cu^{2+}$ ion. Partial amino acid sequence of the enzyme was also determined.

• Archives of Pharmacal Research
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• v.17 no.5
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• pp.318-322
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• 1994

Upon gel filtration, the commercial bovine milk xanthine oxidase preparation was fractionated into two preparations showing enzyme activity. Native polyacrylamide gel electrophoresis showed that one was in a dimeric form and the other was a monomer having molecular weight of 150 kDa. It was also found that this commercial enzyme existed mostly in an active monomeric form without loss of enzyme activity. The rabbit antisera produced against two enzyme preparations cross-reacted well each other. In SDS-polyacrylamide gtel electro-phoresis, however, both enzyme preparations yielded two smaller protein bands below 150 kDa, which appeared to bind with both antisera with high affinity but not to retain enzyme activity. It implies that bovine milk xanthine oxidase can lose its activity when monomeric subunit is further degraded.

• Journal of Sericultural and Entomological Science
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• v.21 no.2
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• pp.7-10
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• 1979

Purified preparations of flacherie virus capsid protein were fractionated by SDS-polyacrylamide gel electrophoresis, and amino acid composition was determined by amino acid analyzer. Three polypeptide components, FP I, FP II and FP III were detected, and the molecular weights of these components were 37,500, 30,500 and 26,500 respectively. The FP III was major poly-peptide comprised about 68.4% of the total virus capsid protein. Seventeen amino acids were detected by an amino acid analyzer from hydrolyzate of the virus capsid protein and the pattern of amino acid composition was similar to those of several other insect viruses.

• The Korean Journal of Zoology
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• v.31 no.2
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• pp.147-155
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• 1988

Six species of false spider mites were collected and ciassifled in South Korea. Among them, a taxonomic description was carried out on the following four species new to Korea: 1. Aegyptobia nothus Pritchard and Baker, 2. Pentomerismus taxi (Hailer), 3. P. oregonensis McGregor, 4. Brevipalpus lewisi McGregor. And also esterase and alkaline phosphatase patterns obtained by polyacrylamide slab gel electrophoresis were compared on some spades. Esterase rymogram showed difference among species in band number and mobility.

• Microbiology and Biotechnology Letters
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• v.19 no.3
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• pp.313-314
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• 1991

- The cyclodextrin glucanotransferase (CGTase) of a mutant of Bacillus stearothermophilus was purified in one step by affinity chromatography. The recovery was 95%. The specific activity of the CGTase increased from 26.2 U/mg protein to 485.5 U/mg protein. The purified CGTase was almost homogeneous by SDS-polyacrylamide gel electrophoresis. The one-step purification proved to be feasible with the mutant in contrast to the parent strain, which required pre-purification step of ammonium sulfate precipitation.

• Korean Journal of Microbiology
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• v.32 no.4
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• pp.297-300
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• 1994

About thirty bacterial strains of actinomycete isolated from the soil were examined for the presence of restriction endonuclease activity. Streptomyces diastatochromogenes, which was identified previously, was found to contain restriction endonuclease activity. The purification of this enzyme, SdiI, was carried out via streptomycin sulfate precipitation and ammonium sulfate fractionation followed by hydroxylapatite column chromatography. Sephacryl S-200 HR column chromatography and second hydroxylapatite column chromatography. SDS-polyacrylamide gel electrophoresis of the active protein (purified from various column chromatography) resulted in 35,000 Da protein.

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.147.2-147.2
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• 2003

A fast and matrix-assisted laser desorption/ionization-mass spectrometry compatible protein staining method in one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis is described. It is based on the counterion dye staining method that employs oppositely charged two dyes, Zincon and Ethyl Violet to form an ion-pair complex. It is safe to use since the methanol used previously in staining solution was replaced with ethanol, which is not toxic. The protocol including fixing, staining and quick washing steps can be completed in 1 to 1.5 h depending upon gel thickness. (omitted)

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.5
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• pp.455-460
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• 1991

In order to identify hard distinct 12 fish species(shiba shrimp Metapenaeus joyneri, fleshy shrimp Penaeus orientalis, ridgetail prawn Palaemon carinicauda, yellow croaker Pseudosciaena manchurica, croaker Niber albiflora, Colichthyes fragilis, brown sole Limanda herzensteini, frog flounder Pleuronichthys cornutrs, Areliscus rhomaleus, stone flounder Kareius bicoloratus, harvest fish Pampus argenteus, flag fish Goniistius zonatus) by seeing with naked eye in Kunsan coastal area, sarcoplasmic protein in the supernatant was used for isoelectric focusing. For getting supernatant, fish muscle tissue was blended with two times deionized water and centrifuged (at $4^{\circ}C$, 12,000rpm for 15min). Isoelectric focusing of sarcoploasmic protein carried out on a LKB Multiphor II using polyacrylamide gel plate (2mm thickness, pH $3.5~10^{\circ}C$, pH 5~8 gradient, at $10^{\circ}C$ for 1.5, 3 hours). In case of uncertain protein pattern, pH gradient was modified to narrow pH gradiet, and excuted 2-D electrophoresis using conventional polyacrylamide gel electrophoresis. Most of fishes except yellow croaker and Collichthyes fragilis were distingushed by isoelectric focusing. The protein maps of 2-D electrophoresis for analyzing two protein bands at aimilar positions(pH 5, 6) between the two fish species showed the diffeences of the estimated molecular weights, 11,700(pH5.0) and 87,000(pH6.0)

• Korean Journal of Microbiology
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• v.28 no.2
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• pp.128-133
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• 1990

The chromatin of all higher eukaryotic cells contains a group of very basic low-mole-cular weight proteins, the histones. But much less is known about histones in lower eukaryotes. Our purpose was to study the histones of the genus Rhizopus. After isolation and purification of nucleoprotein the basic nucleoproteins were analyzed by gel electrophoresis, in sodium dodecyl sulfate as well as acid/urea gels and compared with calf thymus histones. Their electrophoretic mobility in polyacrylamide gel indicate that they are histone homologous, although not identical, to the H2A, H2B, H3 and H4 histones of mammals with the exception of H1. The result suggests that Rhizopus thus appears to contain histone proteins which are homologous to the histones from in higher eukaryotes. The similarity between the calf thymus histone H1 and the Rhizopus high band group remains to be discussed.

• KSBB Journal
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• v.18 no.1
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• pp.35-38
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• 2003

Analysis of proteome in amniotic fluid was performed by 2-D PAGE (polyacrylamide gel electrophoresis). Proteins in amniotic fluid were separated by centrifugation and solubilized in buffer solution for IEF, using an IPG strip of pH 4-7L. Both a homogeneous slab gel of 12.5% and a gradient gel of 8-18%, were used. After 2-D PAGE, spots were stained with silver nitrate and picked up for in-gel digestion. Digested peptides were analyzed by MALDI-TOF and proteins were further identifical. More protein spots were detected in the gradient gels and a protein not previously reported was identified.