A fibrinolytic enzyme from a marine green alga, Codium latum

被引:41
作者
Matsubara, K
Hori, K
Matsuura, Y
Miyazawa, K
机构
[1] Okayama Prefectural Univ, Fac Hlth & Welf Sci, Dept Nutr Sci, Okayama 7191197, Japan
[2] Hiroshima Univ, Fac Appl Biol Sci, Higashihiroshima 7398528, Japan
关键词
Codium latum; fibrinogenolytic activity; fibrinolytic activity; marine alga; molecular weight; optimum pH; protease activity; purification; serine protease;
D O I
10.1016/S0031-9422(99)00356-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A fibrinolytic enzyme was isolated from a marine green alga, Codium latum, and designated C. latum protease (CLP). It also had fibrinogenolytic activity, hydrolyzing A alpha, B beta and gamma chains with preference in this order. As CLP hydrolyzed oxidized insulin B chain at position Arg(22)-Gly(23), and the peptide map of lysozyme digested with CLP was similar to that with trypsin, CLP would be expected to have a high substrate specificity, similar to that of trypsin. Protease activity peaked at pH 10, and was completely inhibited by diisopropyl fluorophosphate (DFP). Therefore, we conclude that CLP is a trypsin-like serine protease. (C) 1999 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:993 / 999
页数:7
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