A pharmacological and biochemical investigation of the venom from the platypus (Ornithorhynchus anatinus).
In this study several activities of the venom of Ornithorhynchus anatinus have been investigated. Whole venom induced local oedema after subplantar injection and produced relaxation of the rat uterus in vitro. The relaxant activity was partially purified by gel permeation HPLC and subsequent analyses by SDS-PAGE revealed that this activity was associated with a 4200 mol. wt peptide. The N-terminal partial sequence of this peptide exhibited substantial identity with human and porcine C-type natriuretic peptide (CNP). Three other major proteins isolated from the venom had mol. wts of 140,000, 55,000 and 16,000. None was found to have any sequence homology with proteins listed in the SwissProt database. The 140,000 mol. wt protein exhibited hyaluronidase activity but the nature of the 55,000 and 16,000 mol. wt proteins remains to be determined. Platypus venom also exhibits protease activity, although the concentration of proteolytic enzymes was too low to be visualised by SDS-PAGE using Coomassie staining.
de Plater
G
G
Division of Botany and Zoology, Australian National University, Canberra.
Martin
R L
RL
Milburn
P J
PJ
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006821:Hyaluronoglucosaminidase / Q000032:analysis; D008297:Male; D008969:Molecular Sequence Data; D010740:Phospholipases / Q000032:analysis; D010987:Platypus; D051381:Rats; D017208:Rats, Wistar; D017386:Sequence Homology, Amino Acid; D013108:Sphingomyelin Phosphodiesterase / Q000032:analysis; D014688:Venoms / Q000737:chemistry* / Q000201:enzymology / Q000494:pharmacology*
D014688:Venoms; D010740:Phospholipases; D013108:Sphingomyelin Phosphodiesterase; D006821:Hyaluronoglucosaminidase