PRIMARY STRUCTURE OF AN INACTIVE MUTANT OF PHOSPHOLIPASE-A(2) IN THE VENOM OF BUNGARUS-FASCIATUS (BANDED-KRAIT)

被引：14

作者：

LIU, CS ^{[1
]}

KUO, PY ^{[1
]}

CHEN, JM ^{[1
]}

CHEN, SW ^{[1
]}

CHANG, CH ^{[1
]}

TSENG, CC ^{[1
]}

TZENG, MC ^{[1
]}

LO, TB ^{[1
]}

机构：

[1] NATL TAIWAN UNIV,INST BIOCHEM SCI,TAIPEI,TAIWAN

来源：

JOURNAL OF BIOCHEMISTRY | 1992年 / 112卷 / 05期

关键词：

D O I：

10.1093/oxfordjournals.jbchem.a123962

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：

From the acidic components of Bungarus fasciatus venom, a very small amount (0.16%) of a novel phospholipase A2 was obtained. Both neurotoxicity and enzyme activity were found to be lacking. Amino acid sequence study showed that it has a normal backbone of group I snake venom phospholipase A2 with 118 amino acid residues. The lack of enzyme activity was attributed to its mutation of the indispensable Asp residue to an Ala residue, ie., the usual His-Asp47 turned out to be His-Ala47. This is the eighth isoform of phospholipase A2 found from the venom of Bungarus fasciatus. Examination of structural homology with three other isoforms revealed 66% similarity at most.

引用

页码：707 / 713

页数：7

共 24 条

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