The lethal and biochemical properties of Bungarus candidus (Malayan krait) venom and venom fractions.
Bungarus candidus venom exhibited high hyaluronidase, acetylcholinesterase and phospholipase A activities; low proteinase, 5'-nucleotidase, alkaline phosphomonoesterase and phosphodiesterase activities and moderately high L-amino acid oxidase activity. SP-Sephadex C-50 ion exchange chromatographic fractionation of the venom and Sephadex G-50 chromatography of the major lethal venom fractions indicate that the venom contains at least two highly lethal, basic phospholipases A with LD50 (i.v.) values of 0.02 micrograms/g (F6A) and 0.18 micrograms/g (F4A), respectively; as well as two polypeptide toxins with LD50 (i.v.) values of 0.17 micrograms/g and 0.83 micrograms/g, respectively. The major lethal toxin is the basic lethal phospholipase A, F6A, which accounts for approximately 13% of the venom protein and has a mol. wt of 21,000.
Tan
N H
NH
Department of Biochemistry, University of Malaya, Kuala Lumpur.
Poh
C H
CH
Tan
C S
CS
D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004546:Elapid Venoms / Q000032:analysis / Q000633:toxicity*; D004798:Enzymes / Q000032:analysis; D007928:Lethal Dose 50; D051379:Mice; D011506:Proteins / Q000032:analysis
D004546:Elapid Venoms; D004798:Enzymes; D011506:Proteins