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• W2055149623 abstract "Phospholipase A2 from Naja nigricollis venom was separated into three fractions by chromatography on a column of CM-Sephadex C-25. The pI values of fractions CMS-5, CMS-6 and CMS-9 were determined to be 7.6, 8.3 and 10.6, respectively. Fraction CMS-9 was further purified on a DEAE-Sephacel column and the homogeneity was verified. The specific activity of CMS-9 was found to be 1300 units per mg and lethal toxicity 0.3 mg per kg mouse. The most basic and toxic fraction, CMS-9, was subjected to chemical modification with p-bromophenacyl bromide. The enzyme lost both the enzyme activity and lethal toxicity, however, the antigenicity remained unchanged. Although both 8-anilinonaphthalenesulfonate and Ca2+ showed pronounced protection on the inactivation process, the mechanism of 8-anilinonaphthalene-sulfonate protection is different from that of Ca2+. Amino acid analysis showed that only one (His-47) out of three histidine residues was modified. Although both native and His-modified CMS-9 were perturbed by the presence of Ca2+, the modified enzyme lost the characteristic tryptophan blue shift suggesting that the modified enzyme is unable to exert a charge effect upon Ca2+ binding in the vicinity of the tryptophan group. Scatchard plots revealed only one type of binding sites for 8-anilinonaphthalenesulfonate in the presence of CA2+. On the other hand, the modified enzyme lost the ability to bind 8-anilinonaphthalene. It is suggested tentatively that the hydrophobic pocket in which 8-anilinonaphthalenesulfonate is bound may be the site of the enzyme that interacts with phospholipid." @default.
• W2055149623 created "2016-06-24" @default.
• W2055149623 creator A5058902203 @default.
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• W2055149623 date "1980-08-01" @default.
• W2055149623 modified "2023-10-15" @default.
• W2055149623 title "Chemical modification of the histidine residue in basic phospholipase A2 from the venom of naja nigricollis" @default.
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• W2055149623 doi "https://doi.org/10.1016/0005-2744(80)90227-2" @default.
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