Isolation, partial characterization and complete amino acid sequence of the toxic phospholipase A2 from the venom of the common viper, Vipera berus berus

I Krizaj; J Siigur; M Samel; V Cotic; F Gubensek

doi:10.1016/0304-4165(93)90081-i

Isolation, partial characterization and complete amino acid sequence of the toxic phospholipase A2 from the venom of the common viper, Vipera berus berus

Biochim Biophys Acta. 1993 May 7;1157(1):81-5. doi: 10.1016/0304-4165(93)90081-i.

Authors

I Krizaj¹, J Siigur, M Samel, V Cotic, F Gubensek

Affiliation

¹ Department of Biochemistry, J. Stefan Institute, Ljubljana, Slovenia.

PMID: 8499481
DOI: 10.1016/0304-4165(93)90081-i

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Chromatography, Liquid
Molecular Sequence Data
Phospholipases A / chemistry
Phospholipases A / isolation & purification*
Phospholipases A2
Sequence Homology, Amino Acid
Viper Venoms / enzymology*

Substances

Viper Venoms
Phospholipases A
Phospholipases A2