A comparative study of the biological properties of krait (genus Bungarus) venoms

Comp Biochem Physiol C Comp Pharmacol Toxicol. 1990;95(1):105-9. doi: 10.1016/0742-8413(90)90089-r.

Abstract

1. The intravenous median lethal doses (LD50), protease, phosphodiesterase, alkaline phosphomonoesterase, L-amino acid oxidase, acetylcholinesterase, phospholipase A, 5'-nucleotidase, hyauronidase and anticoagulant activities of fourteen samples of venoms from the four common species of krait (Bungarus caeruleus, Bungarus candidus, Bungarus multicinctus and Bungarus fasciatus) were examined. 2. The results indicate that even though there are individual variations in the biological properties of the krait venoms, interspecific differences in the properties can be used for differentiation of the venoms from the four species of Bungarus. Particularly useful for this purpose are the LD50's and the contents of 5'-nucleotidase and hyaluronidase of the venoms.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 5'-Nucleotidase / metabolism
  • Acetylcholinesterase / metabolism
  • Alkaline Phosphatase / metabolism
  • Amino Acid Oxidoreductases / metabolism
  • Animals
  • Anticoagulants
  • Carboxylic Ester Hydrolases / metabolism
  • Coagulants
  • Elapid Venoms / pharmacology*
  • Hemorrhage / chemically induced
  • Hyaluronoglucosaminidase / metabolism
  • L-Amino Acid Oxidase
  • Lethal Dose 50
  • Mice
  • Peptide Hydrolases / metabolism
  • Phospholipases A / metabolism
  • Phosphoric Diester Hydrolases / metabolism
  • Species Specificity

Substances

  • Anticoagulants
  • Coagulants
  • Elapid Venoms
  • Amino Acid Oxidoreductases
  • L-Amino Acid Oxidase
  • arginine esterase
  • Carboxylic Ester Hydrolases
  • Phospholipases A
  • Acetylcholinesterase
  • Alkaline Phosphatase
  • 5'-Nucleotidase
  • Phosphoric Diester Hydrolases
  • Hyaluronoglucosaminidase
  • Peptide Hydrolases