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 et al., ISOLATION, PARTIAL CHARACTERIZATION AND COMPLETE AMINO-ACID-SEQUENCE OF THE TOXIC PHOSPHOLIPASE-A2 FROM THE VENOM OF THE COMMON VIPER, VIPERA-BERUS-BERUS, Biochimica et biophysica acta, 1157(1), 1993, pp. 81-85
A basic, toxic phospholipase A2 was purified from the venom of Vipera
berus berus (Vbb) by a single purification step, using hydrophobic chr
omatography. The primary structure of isolated protein was established
from peptides generated by Gly-specific papaya proteinase IV, beta-tr
ypsin, CNBr and mild acid hydrolysis. The enzyme consists of a single
chain of 122 amino acid residues with 14 Cys in positions characterist
ic for the phospholipase A2 subgroup IIA. As far as we know, this is t
he first complete Vipera berus phospholipase A2 amino acid sequence re
ported.