Purification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venom

Int J Biochem. 1990;22(5):481-7. doi: 10.1016/0020-711x(90)90261-z.

Abstract

1. The two major phospholipase A2 enzymes (OHPLA-DE1 and OHPLA-DE2) of king cobra (Ophiophagus hannah) venom have been purified to electrophoretic homogeneity. 2. The isoelectric points of OHPLA-DE1 and OHPLA-DE2 were 3.81 and 3.89, respectively and the Mws were 14,000 and 15,000, respectively, as estimated by Sephadex G-75 gel filtration chromatography; and 14,000 as estimated by SDS-PAGE. 3. The enzymes were not lethal to mice at a dosage of 10 micrograms/g body wt by i.v. route. Both phospholipase A2 enzymes, however, exhibited moderate edema-inducing and anti-coagulant activities. 4. Bromophenacylation of the enzymes reduced the enzymatic activity drastically but did not affect the edema-inducing activity of the enzymes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetophenones
  • Animals
  • Blood Coagulation / drug effects
  • Chemical Phenomena
  • Chemistry
  • Chromatography, Gel
  • Edema / chemically induced
  • Elapid Venoms / analysis*
  • Electrophoresis, Polyacrylamide Gel
  • Isoelectric Point
  • Mice
  • Molecular Weight
  • Phospholipases / isolation & purification*
  • Phospholipases A / isolation & purification*
  • Phospholipases A / pharmacology
  • Phospholipases A / toxicity
  • Phospholipases A2

Substances

  • Acetophenones
  • Elapid Venoms
  • Phospholipases
  • Phospholipases A
  • Phospholipases A2
  • 4-bromophenacyl bromide