HUMAN ERYTHROCYTE MULTICATALYTIC PROTEINASE - ACTIVATION AND BINDING TO SULFATED GALACTOSYLCERAMIDES AND LACTOSYLCERAMIDES

被引：28

作者：

OHKUBO, I

GASA, S

NAMIKAWA, C

MAKITA, A

SASAKI, M

机构：

[1] NAGOYA CITY UNIV,SCH MED,DEPT BIOCHEM,NAGOYA,AICHI 467,JAPAN

[2] HOKKAIDO UNIV,SCH MED,INST CANC,BIOCHEM LAB,SAPPORO,HOKKAIDO 060,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 174卷 / 03期

关键词：

D O I：

10.1016/0006-291X(91)91538-N

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：

Chymotrypsin-like activity of multicatalytic proteinase (MCP) purified from human erythrocytes was selectively activated 2.5 - 3.5-fold by sulfated glycolipids such as galactosylceramide sulfate (SM4) and lactosylceramide sulfate (SM3) but not by other glycolipids including galactosylceramide (GalCer), lactosylceramide (LacCer), GDla, GMl and GM3. Heparin also selectively activated trypsin-like activity 2.5-fold, while other mucopolysaccharides did not. This proteinase molecule bound specifically and with high affinity to both SM4 and SM3, but not to GalCer, LacCer and GM3. The binding of SM4 and SM3 to the enzyme molecule was also confirmed by thin layer chromatography. © 1991.

引用

页码：1133 / 1140

页数：8

共 33 条

[11] ISOLATION OF 2 FORMS OF THE HIGH-MOLECULAR-MASS SERINE PROTEASE, INGENSIN, FROM PORCINE SKELETAL-MUSCLE [J].