ISOLATION, PARTIAL CHARACTERIZATION AND COMPLETE AMINO-ACID-SEQUENCE OF THE TOXIC PHOSPHOLIPASE-A2 FROM THE VENOM OF THE COMMON VIPER, VIPERA-BERUS-BERUS

被引：17
作者：
KRIZAJ, I
SIIGUR, J
SAMEL, M
COTIC, V
GUBENSEK, F
机构：
[1] J STEFAN INST,DEPT BIOCHEM,JAMOVA 39,POB 100,61111 LJUBLJANA,SLOVENIA
[2] INST CHEM PHYS & BIOPHYS,TALLINN,ESTONIA
来源：
BIOCHIMICA ET BIOPHYSICA ACTA | 1993年 / 1157卷 / 01期
关键词：
ENZYME PURIFICATION; PHOSPHOLIPASE-A2; TOXIN; PRIMARY STRUCTURE; (VIPERA-BERUS-BERUS); (SNAKE VENOM);
D O I：
10.1016/0304-4165(93)90081-I
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 basic, toxic phospholipase A2 was purified from the venom of Vipera berus berus (Vbb) by a single purification step, using hydrophobic chromatography. The primary structure of isolated protein was established from peptides generated by Gly-specific papaya proteinase IV, beta-trypsin, CNBr and mild acid hydrolysis. The enzyme consists of a single chain of 122 amino acid residues with 14 Cys in positions characteristic for the phospholipase A2 subgroup IIA. As far as we know, this is the first complete Vipera berus phospholipase A2 amino acid sequence reported.
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页码：81 / 85
页数：5
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