Characterization of phospholipase A2 from the venom of Horned viper (Cerastes cerastes).

Abstract:

: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).

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Siddiqi AR,Shafqat J,Zaidi ZH,Jörnvall H

doi

10.1016/0014-5793(91)80072-b

subject

Has Abstract

pub_date

1991-01-14 00:00:00

pages

14-6

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)80072-B

journal_volume

278

pub_type

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