PURIFICATION AND PROPERTIES OF A NOVEL LATENT PROTEINASE SHOWING MYOSIN HEAVY-CHAIN DEGRADING ACTIVITY FROM THREADFIN-BREAM MUSCLE

被引：69

作者：

KINOSHITA, M

TOYOHARA, H

SHIMIZU, Y

机构：

[1] Department of Fisheries, Faculty of Agriculture, Kyoto University, Kyoto, Kyoto 606, Sakyo-ku

来源：

JOURNAL OF BIOCHEMISTRY | 1990年 / 107卷 / 04期

关键词：

D O I：

10.1093/oxfordjournals.jbchem.a123090

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 novel latent proteinase of which activity was induced by heating in the presence of NaCl was purified to homogeneity from threadfin-bream muscle by a combination of DEAE-cellulose, Con A-Sepharose, Arg-Sepharose, and Shim-pack HAC chromatographies. This proteinase was a glycoprotein having a monomeric subunit structure; Mr was estimated to be 77, 000 on SDS-PAGE analysis. The proteinase hydrolyzed Boc-Leu-Thr-Arg-MCA as well as myosin heavy chain in the presence of 2-4% NaCl at pH 7.0 and at 60°C, optimally. The proteinase was classified as serine proteinase based on the effects of soybean trypsin inhibitor, leupeptin, and antipain. © 1990 COPYRIGHT, 1990 BY THE JOURNAL OF BIOCHEMISTRY.

引用

页码：587 / 591

页数：5

共 18 条

[1]

Barrett A.J., 1977, PROTEINASES MAMMALIA, P1

[2] IDENTIFICATION OF 2 ALKALINE PROTEASES AND A TRYPSIN-INHIBITOR FROM MUSCLE OF WHITE CROAKER (MICROPOGON-OPERCULARIS) [J].