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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
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Purification and some properties of alkaline proteinases in the pyloric caeca of skipjack, Katsuwonus vagans, were investigated. Four alkaline proteinases, temporarily designated proteinases I, II, III and IV, were identified from the tissue extract of the pyloric caeca by ammonium sulfate fractionation, DEAF-Sephadex A-50 chromatography, and Sephadex G-100 and G-200 gel filtration. Result of disc-polyacrylamide gel electrophoretic analysis showed that the purified proteinases II and III were homogenous with the yields of 1.5% and 1.2%, and those specific activities were increased to 33 to 37 fold over that of the crude enzyme solution, respectively. Molecular weight of the proteinases II and III determined by sephadex G-100 gel filtration were 28,500 and 24,200, respectively. The optimum conditions for the caseinolytic activity of the two enzymes were pH 9.6 and 48℃. The reaction rates of the two alkaline proteinases were constant to the reaction time to 80 min in the reaction mixture of 3.4㎍/㎖ of enzyme concentration and 2% casein solution. The Km values against casein substrate determined by the method of Lineweaver-Burk were 0.56% for proteinase II and 0.30% for proteinase III. The proteinases II and III were inactivated under the presence of Ag^+, Hg^(2+), Ni^(2+), Fe^(2+), and Cu^(2+), but activated by Mn^(2+) and Ca^(2+), and markedly inhibited by the soybean trypsin inhibitor and N-p-toluenesulfonyl-L-lysine chloromethyl ketone. Therefore, the proteinases II and III were found to be a group of serine proteases and assured to be trypsin-like proteinases.
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