Open AccessPurification and characterization of two highly different group II phospholipase A 2 isozymes from a single viperid ( Eristocophis macmahoni ) venom
Author(s) -
SIDDIQI Abdur Rehman,
ZAIDI Zafar H.,
JÖRNVALL Hans
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb16328.x
Subject(s) - isozyme , venom , fast protein liquid chromatography , biology , phospholipase , biochemistry , viperidae , enzyme , phospholipase a2 , phospholipase a
Two phospholipase A 2 isozymes have been purified from leaf‐nosed viper by gel permeation chromatography followed by reverse‐phase HPLC and cation‐exchange FPLC. Both enzymes contain seven pairs of half‐cystine, typical of group II phospholipase A 2 . Surprisingly large difference, affecting both N‐ and C‐terminal regions, exist between the two isozymes purified from the same snake venom. Exchanges occur at no less than 27 of 121 positions (22%), suggesting the possible existence of two genes for phospholipase A 2 . The residue identity with the enzymes from other Viperidae species is also low, only 44–48%, indicating extensive of this protein structure at large. Functionally, the present isozymes do not possess the cationic regions ascribed to myotoxicity and anti‐coagulant effects of the enzyme.