• Applied Biological Chemistry
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• 제24권2호
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• pp.149-152
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• 1981

Lactobacillus bulgaricus 균체(菌體)의 고정화방법(圖定化方法)으로서 polyacrylamide gel과 Al- Ca-, Fe- 및 Mg-alginate bead에 대하여 고찰하고 이중 가장 활성이 좋은 것은 Ca-alginate bead 이었으며 입경(粒經) 2m/m로 형성시킨 Ca-alginate bead로 고정화(圖定化)시킨 균류(菌類)의 경우, 4.5% lactose 용액 및 whey에서의 lactose 분해실험 결과, 생균(生菌)에 대비(對比)한 상대적 활성은 각각 최고 28% 및 18% 이었다.

• 한국식품과학회지
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• 제14권2호
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• pp.106-111
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• 1982

대두 7품종과 이를 이면교잡(二面交雜)해서 얻은 2대 21종의 대두에서 각각 가용성 단백질을 추출하여 Sephadex G-75에 의한 겔 여과와 polyacrylamide 겔 전기영동으로 트립신 인히비터를 분획 정제한 결과 16종의 트립신 인히비터가 검출되었고 각종류의 대두마다 $5{\sim}12$종의 트립신 인히비터가 존재하였으며 주로 5종의 트립신 인히비터가 분포하였다.

• 한국미생물·생명공학회지
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• 제27권6호
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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.

• 한국산학기술학회논문지
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• 제3권4호
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• pp.251-256
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• 2002

폴리머용액의 특성확산시간은 낙구의 종말속도를 측정함으로써 결정할 수 있다. 확산시간은 폴리머 용액의 농도가 증가할수록 증가한다. 입자영상유속장치 (PIV)를 이용하여 구주위의 유동현상을 가시화 하였다. 2000 ppm의 경우 30 초 간격으로 떨어뜨렸을때의 속도가 0초( 처음)나 40초후, 50초후에 떨어뜨렸을때와 비교하여 가장 크게 나타났다. 뉴톤 유체에서는 낙구의 전방과 후방에서 구주위의 유동장이 동일하게 나타났다.

• Journal of Plant Biology
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• 제32권4호
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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.

• 약학회지
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• 제30권6호
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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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• 제17권5호
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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.

• 약학회지
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• 제36권3호
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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.

• 한국잠사곤충학회지
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• 제21권2호
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• pp.7-10
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• 1979

1. 연화병 바이러스의 단백질을 SDS-polyacrylamide gel 전기영동으로 분석한 결과 분자량 37,500(FP I), 30,500(FP II) 및 26,500(FP III)에 상당하는 3종류의 polypeptide가 얻어졌으며, 이들의 비율은 FP I이 6.6%, FPII가 25.0% 및 FP III가 68.4%였다. 2. 연화병 바이러스의 단백질을 amino산 분석을 행한 결과, 17종의 amino산이 분리되었으며, 이 amino산 조성은 타곤충 바이러스의 amino산 조성과 유사하였다.

• 한국펄프종이공학회:학술대회논문집
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• 한국펄프종이공학회 1999년도 Pre-symposium of the 10th ISWPC Recent Advances in Paper Science and Technology
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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.