COMPARISON OF PHYTOLACAIN-R, A CYSTEINE PROTEASE FROM PHYTOLACCA-AMERICANA, WITH PAPAIN

被引：14

作者：

KANEDA, M

NAGATOME, S

UCHIKOBA, T

机构：

[1] Department of Chemistry, Faculty of Science, Kagoshima University, Kagoshima, 890, Korimoto

来源：

PHYTOCHEMISTRY | 1995年 / 39卷 / 05期

关键词：

PHYTOLACCA AMERICANA; PHYTOLACCACEAE; POKEWEED; CYSTEINE PROTEASE; PHYTOLACAIN R;

D O I：

10.1016/0031-9422(95)00163-2

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：

Nine sites of oxidized insulin B-chain were cleaved by phytolacain R, isolated from pokeweed, after 20 hr of hydrolysis. Five cleavage sites resembled those of papain. Substrate specificity of phytolacain R was similar to that of papain, preferring hydrophobic P-2 residues. The activities of fibrin formation and elastin hydrolysis of phytolacain R were higher than those of papain. The amino terminal sequence of phytolacain R, although similar was not identical with that of papain.

引用

页码：997 / 999

页数：3

共 11 条

[1]

Arima K., 1970, METHODS ENZYMOLOGY, V19, P446, DOI 10.1016/0076-6879(70)19033-1

[2] CYSTEINE PROTEASES - THE S2P2 HYDROGEN-BOND IS MORE IMPORTANT FOR CATALYSIS THAN IS THE ANALOGOUS S1P1 BOND [J].