4.6 Article

Identification of β-type phospholipase A2 inhibitor in a nonvenomous snake, Elaphe quadrivirgata

期刊

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 408, 期 1, 页码 124-130

出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0003-9861(02)00551-9

关键词

phospholipase A(2); phospholipase A(2) inhibitor; snake serum; leucine-rich repeats; amino acid sequence; cDNA cloning

向作者/读者索取更多资源

A novel serum protein inhibiting specifically the enzymatic activity of the basic phospholipase A (PLAN) from the venom of the Chinese mamushi snake (Agkistrodon blomhoffii siniticus) was purified from a nonvenomous Colubridae snake, Elaphe quadrivirgata. The purified inhibitor was a 150-kDa glycoprotein having a trimeric structure, composed of two homologous 50-kDa subunits. Their amino acid sequences, containing leucine-rich repeats, were typical of the beta-type PLA2 inhibitor (PLIbeta), previously identified from the serum of A. blomhoffii siniticus. The inhibitor inhibited exclusively group II basic PLA(2)s and did not inhibit other kinds of PLA(2)s. This is the first paper reporting the existence of PLIbeta in a nonvenomous snake. The existence of PLIbeta in the nonvenomous snake reflects that PLIbetas are widely distributed over the snake species and participate commonly in regulating the physiological activities of the unidentified target PLA(2)s. (C) 2002 Elsevier Science (USA). All rights reserved.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.6
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据