Purification of a proteinase (Ac5-proteinase) and characterization of hemorrhagic toxins from the venom of the hundred-pace snake (Agkistrodon acutus).
Ac5-Proteinase (15.2 mg) was isolated from Agkistrodon acutus venom (1 g) by column chromatography on Sephadex G-75, CM-Sephadex C-50 and CM-Cellulose. Ac5-Proteinase was homogeneous by disc electrophoresis on polyacrylamide gel at pH 4.3 and also by SDS-disc polyacrylamide gel electrophoresis. Ac1-, Ac2-, Ac3- and Ac5-proteinases possessed lethal and hemorrhagic activities, but Ac4-proteinase had no lethal activity. These activities were inhibited completely by ethylenediaminetetraacetic acid (EDTA), 1,10-phenanthroline or cysteine. The molecular weights of Ac1-, Ac2-, Ac3-, Ac4- and Ac5-proteinases were approximately 24,500, 25,000, 57,000, 33,000 and 24,000, respectively. Ac1-, Ac2-, Ac4- and Ac5-proteinases did not contain any carbohydrates, but Ac3-proteinase contained 0.1% carbohydrate by weight.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D003435:Crotalid Venoms / Q000032:analysis* / Q000633:toxicity; D010450:Endopeptidases / Q000302:isolation & purification*; D006470:Hemorrhage / Q000139:chemically induced*; D006358:Hot Temperature; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D007928:Lethal Dose 50; D051379:Mice; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D011817:Rabbits
D000596:Amino Acids; D003435:Crotalid Venoms; D010450:Endopeptidases; D010447:Peptide Hydrolases; C042149:Ac5-proteinase