Isolation, partial characterization and complete amino acid sequence of the toxic phospholipase A2 from the venom of the common viper, Vipera berus berus.
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.
Department of Biochemistry, J. Stefan Institute, Ljubljana, Slovenia.
I
I
Krizaj
J
J
Siigur
M
M
Samel
V
V
Cotic
F
F
Gubensek
D000595:Amino Acid Sequence; D002853:Chromatography, Liquid; D008969:Molecular Sequence Data; D010741:Phospholipases A / Q000737:chemistry / Q000302:isolation & purification*; D054467:Phospholipases A2; D017386:Sequence Homology, Amino Acid; D014757:Viper Venoms / Q000201:enzymology*
D014757:Viper Venoms; D010741:Phospholipases A; D054467:Phospholipases A2