• Applied Biological Chemistry
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• v.24 no.2
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• pp.149-152
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• 1981

The immobilization of Lactobacillus bulgaricus was investigated by various method, e.g. by use of polyacrylamide gel and Al-, Ca-, Fe- or Mg-alginate beads, and the most active immobilized cells were obtained by entrapment in a Ca-alginate beads. These immobilized microbial cells, when introduced into 4.5% lactose solution and whey solution showed maximum relative activity of 28% or lactose solution and 18% for whey solution as measured against the native microbial reference standard (100).

• Korean Journal of Food Science and Technology
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• v.14 no.2
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• pp.106-111
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• 1982

To investigate the soybean trypsin inhibitors from seven varieties of soybeans and their twenty one $F_1-hybrids$, water soluble proteins were extracted. Trypsin inhibitors were isolated from those proteins and purified by sephadex G-75 column chromatography and polyacrylamide gel electrophresis. Total 16 kinds of trypsin inhibitors were isolated. From each variety of soybeans, $5{\sim}12$ kinds of trysin inhibitors could be detected and among them, 5 kinds of trypsin inhibitors were mainly distributed.

• Microbiology and Biotechnology Letters
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• v.27 no.6
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• pp.471-476
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• 1999

Inulin fructotransferase(depolymerizing)(EC 2.4.1.93)(inulaseII) which converts inulin into di-D-fructofuranose-1,2':2,3'-dianhydride (DFAIII) was purified from Arthrobacter ureafaciens KCTC 3387 using column chromatography on DEAE-Toyopearl 650M and gel filtration of Sephadex G-200. The enzyme was purified 7-fold with a yield of 11% from a culture supernatant. The purified enzyme gave a single band on polyacrylamide gel electrophoresis, and the molecular weight of the enzyme was estimated to be 45,000 by SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature for the enzyme reaction were pH6.5~7.0 and $55{\circ}C$, respectively. The enzyme was stable within a pH range of 5.0 to 10.6 and up to $60^{\circ}C$. The Km of this enzyme for DFAIII production was 11.9mM. The enzyme was inactivated by $Hg^{2+}$ and after exhaustive digestion of inulin by this enzyme, 1-kestose and nystose were produced in addition of DFAIII.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.3 no.4
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• pp.251-256
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• 2002

The average diffusion time of a polyacrylamide solution was determined by measuring the terminal velocities of the falling balls. The diffusion time increased as the polyacrylamide concentration increased. The PIV (Particle Image Velocimetry) system was employed to visualize the flow phenomena around balls. For a time interval of 30 seconds in the 2000 wppm, velocity vectors were larger than in case of 0 seconds, 40 seconds and 50 seconds in the falling ball. However, in the Newtonian fluid, flow vsualization around balls were performed at both upstream and downstream of the falling ball.

• Journal of Plant Biology
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• v.32 no.4
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• pp.331-341
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• 1989

DNA methyltransferase was purified 282.6-fold from Chlamydomonas reinhardtii 21gr (mt+) gametic cell to examine the effect of polyamine on the enzyme acctivity. Polyacrylamide gel electrophoresis(PAGE) revealed at least three bands(1 major band, 2 minor bands). Among these, the major band represents DNA methyltransferase. Polyacrylamide gel electrophoresis in the presence of 0.1% sodium dodecylsulfate(SDS-PAGE) revealed a major band with M.W. 60,000. DNA methyltransferase activity was inhibited more effectively by spermine than by spermidine, and the inhibition by putrescine was smaller than spermine and spermidine. DNA methyltransferase activity was inhibited by 40% and 53% at 5mM and 20mM spermine, respectively. In the case of spermidine, the inhibition was 35% at 10mM and 44% at 20mM. However, the inhibition by putrescine appeared only above 5mM and reached about 25% at 20mM.

• YAKHAK HOEJI
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• v.30 no.6
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• pp.343-347
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• 1986

Korean ginseng was purified to obtain radioprotective protein fractions by buffer extraction, ammonium sulfate fractionation, CM-cellulose column chromatography, heat inactivation and Sephadex G-75 column chromatography. The final three fractions, GI, GII and GIII were subjected to Disc-polyacrylamide gel electrophoresis (PAGE) and SDS-PAGE. The molecular weights(M.W.) of native and denatured proteins were estimated by using regression line equations obtained from the mobilities of standard proteins. As the results, in Disc-PAGE, the GI fraction showed two protein bands with M.W. of above 213, 000 and 55, 000, GII showed one band with M.W. of 44, 000 and GIII, also one band with M.W. of 19, 000. In SDS-PAGE, GI fraction gave four subunit bands with M.W. of above 114, 000, 27, 000, 24, 000 and 19, 000, GII gave two bands with M.W. of 46, 000 and 22, 000, and GIII, one band of 19, 000.

• 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.

• YAKHAK HOEJI
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• v.36 no.3
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• pp.241-249
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• 1992

The whole body extract of Lunella coronata coreensis agglutinated nonspecifically human and other animal erythrocytes. A new lectin was purified by the following procedures: 0.15 M NaCl extraction, salt fractionation, gel filtration, anionic and cationic ion exchange column chromatographies. Through these purification procedures, specific activity of LCC-I was increased from 276 to 9714.3 units/mg, And on polyacrylamide gel electrophoresis, LCC-I exhibited one major band. A molecular weight of LCC-I was assumed to be 20,000 by sodium dodesyl sulfate polyacrylamide gel electrophoresis. The purified lectin was relatively stable at various pH and heat. Among the tested sugars, lactose and lactulose inhibited lectin activity at a concentration of 6.25 mM, respectively.

• 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.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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• 1999.04b
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• pp.276-281
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• 1999

The surfaces of sheets added with N-chloro-polyacrylamide (N-Cl-PAM) are analyzed using X-ray photoelectron spectroscopy (XPS) to clarify the chemical bonding involved in the paper strength development induced by N-Cl-PAM. The comparison of the observed N1s chemical shift of the sheet with those of the paper strength additives and the model compound, 1-butyryl-3-propyl urea, illustrated the presence of covalent bonds of alkyl acyl urea and urethane on the fiber surfaces. Thus the formation of the covalent bonds by N-Cl-PAM themselves and by N-Cl-PAM with cellulose and hemicellulose may be an explanation for much higher effectiveness of N-Cl-PAM on the improvement of wet strength of paper than A-PAM.