Characterization of phospholipase A2 from the venom of Horned viper (Cerastes cerastes).
Phospholipase A2 has been purified from the venom of Horned viper (Cerastes cerastes) by gel permeation chromatography followed by reverse-phase HPLC. The primary structure was established by sequence analysis of the intact protein and its enzymic peptides. The structure has 120 residues, properties like other group IIB phospholipases, but only 45-55% identity with the enzyme from other viperid species, and large variations even within the species (26% residue differences at known positions in another form).
Siddiqi
A R
AR
Department of Chemistry I, Karolinska Institutet, Stockholm, Sweden.
Shafqat
J
J
Zaidi
Z H
ZH
Jörnvall
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010741:Phospholipases A / Q000737:chemistry*; D054467:Phospholipases A2; D012689:Sequence Homology, Nucleic Acid; D014757:Viper Venoms / Q000378:metabolism*
D014757:Viper Venoms; D010741:Phospholipases A; D054467:Phospholipases A2