title: A comparative study of the biological properties of Australian elapid venoms.
abstract: 1. The hemorrhagic, procoagulant, anticoagulant, protease, phosphodiesterase, alkaline phosphomonoesterase, L-amino acid oxidase, acetylcholinesterase, arginine ester hydrolase, phospholipase A, 5'-nucleotidase and hyaluronidase activities of 39 samples of venoms from 13 species (15 taxa) of Australian elapids were determined and the Sephadex G-75 gel filtration patterns for some of the venoms were also examined. 2. The results indicate that Australian elapid venoms can be divided into two groups: procoagulant Australian venoms (including N. scutatus, N. ater, O. scutellatus, O. microlepidotus, P. porphyriacus, T. carinatus, H. stephensii and P. textilis) and non-procoagulant Australian venoms (including A. superbus, P. colletti, P. australis, P. guttatus and A. antarcticus). 3. The non-procoagulant Australian venoms exhibited biological properties similar to other elapid venoms, while the procoagulant Australian venoms exhibited some properties characteristic of viperid venoms. 4. The data show that information on venom biological properties can be used for differentiation of many species of Australian elapids. 5. Particularly useful for this purpose are the hyaluronidase, alkaline phosphomonoesterase, acetylcholinesterase, and the procoagulant activities and the Sephadex G-75 gel filtration patterns of the venoms.
authors.affiliation: Department of Biochemistry, University of Malaya, Kuala Lumpur.
authors.forename: N H
authors.initials: NH
authors.lastname: Tan
authors.forename: G
authors.initials: G
authors.lastname: Ponnudurai
mesh_terms: D000818:Animals; D001315:Australia; D002850:Chromatography, Gel; D004546:Elapid Venoms / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology / Q000633:toxicity*; D006867:Hydrolases / Q000302:isolation & purification / Q000378:metabolism; D012911:Snakes; D013045:Species Specificity
chemical_list: D004546:Elapid Venoms; D006867:Hydrolases