Cucumisin-like protease from the latex of Euphorbia supina

被引：45

作者：

Arima, K ^{[1
]}

Uchikoba, T ^{[1
]}

Yonezawa, H ^{[1
]}

Shimada, M ^{[1
]}

Kaneda, M ^{[1
]}

机构：

[1] Kagoshima Univ, Fac Sci, Dept Chem, Kagoshima 8900065, Japan

来源：

PHYTOCHEMISTRY | 2000年 / 53卷 / 06期

关键词：

Euphorbia supina; Euphorbiaceae; cucumisin; serine protease; plant protease;

D O I：

10.1016/S0031-9422(99)00605-6

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 protease has been purified From the latex of Euphorbia supina Rafin by two steps of chromatography. The M-t, was estimated by SDS-PAGE to be 80 kDa. Its activity was inhibited strongly by diisopropyl fluorophosphate: but not by EDTA, pepstatin, or cysteine protease inhibitors, indicating that the enzyme is a serine protease. The specificity of the protease is broad, but the preferential cleavage sites were C-terminal sites of hydrophobic amino acid residues. The N-terminal sequence of the first fifteen residues was determined and six of the residues match those in cucumisin [EC 3.4.21.25], a protease from the sarcocarp of melon fruit (Cucumis melo L. var. Prince). The results indicate that the E. supina Protease is a cucumisin-like serine protease. (C) 2000 Elsevier Science Ltd. All rights reserved.

引用

页码：639 / 644

页数：6

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