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Characterization of phospholipase A2 from the venom of Horned viper ( Cerastes cerastes )
Author(s) -
Abdur Rehman Siddiqi,
Jawed Shafqat,
Zafar H. Zaidi,
Hans Jörnvall
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80072-b
Subject(s) - venom , viper venoms , viper , ophidia , biology , viperidae , residue (chemistry) , phospholipase a2 , phospholipase a , biochemistry , snake venom , chemistry , enzyme
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).