PURIFICATION AND CHARACTERIZATION OF A PROTEINASE IDENTIFIED AS CATHEPSIN-D FROM TILAPIA MUSCLE (TILAPIA-NILOTICA X TILAPIA-AUREA)

被引：14

作者：

JIANG, ST ^{[1
]}

WANG, YT ^{[1
]}

CHEN, CS ^{[1
]}

机构：

[1] ACAD SINICA,INST BOT,TAIPEI 11529,TAIWAN

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 1991年 / 39卷 / 09期

关键词：

D O I：

10.1021/jf00009a011

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

For understanding the characteristics of lysosomal enzymes, cathepsin D was first purified by heat treatment, concanavalin A-Sepharose and Sephadex G-150 chromatographies, and finally preparative electrophoresis. A purification of 244-fold against the crude extract was achieved. The recovery was 2%. The purified enzyme appeared to be electrophoretically homogeneous and had a molecular weight of 55 000. Inhibitor study and molecular weight determination indicated this enzyme to be an aspartic proteinase, cathepsin D. The optimal pH and temperature were 3.5 and 37-degrees-C, respectively. This proteinase was inhibited by Hg2+ and Fe3+ but activated by Ca2+, Ni2+, and Mg2+ and slightly activated by Zn2+ and Cd2+. The purified cathepsin D was completely inhibited by pepstatin, partially inhibited by p-(chloromercuri)benzoate (PCMB), and ethylenediaminetetraacetic acid (EDTA), and almost not affected by 2-mercaptoethanol.

引用

页码：1597 / 1601

页数：5

共 32 条

[21]

LOWRY OH, 1951, J BIOL CHEM, V193, P265

[22]

MAKINODAN Y, 1976, B JPN SOC SCI FISH, V42, P239

[23]

MAKINODAN Y, 1982, B JPN SOC SCI FISH, V48, P1501

[24] MODE OF DEGRADATION OF MYOFIBRILLAR PROTEINS BY RABBIT MUSCLE CATHEPSIN-D [J].