title: Purification and characterization of a fibrinogenase from the venom of Western Diamondback rattlesnake (Crotalus atrox).
abstract: A fibrinogenolytic enzyme was isolated from the venom of Western Diamondback rattlesnake (Crotalus atrox) by a three-step procedure involving gel filtration and anion-exchange chromatography. The molecular weight was estimated as 22 900 by SDS-polyacrylamide gel electrophoresis. The isoelectric point was found to be pH 4.65. The enzyme rapidly destroyed the ability of bovine fibrinogen to form a clot on incubation with thrombin. Incubation of fibrinogen with the fibrinogenolytic enzyme for 5 min resulted in the disappearance of the beta-chain of fibrinogen and the appearance of lower molecular weight fragments. Thus the enzyme can be classified as a beta-fibrinogenase. However, on prolonged incubation of the fibrinogen there was also a partial digestion of the alpha-chain. The fibrinogenase showed no activity towards fibrin or casein or arginine esters. The fibrinogenolytic activity was inhibited by phenylmethanesulphonyl fluoride (PMSF) but was unaffected by EDTA.
mesh_terms: D000818:Animals; D002417:Cattle; D003435:Crotalid Venoms / Q000302:isolation & purification*; D005340:Fibrinogen / Q000502:physiology; D005342:Fibrinolysis; D007700:Kinetics; D008970:Molecular Weight; D012911:Snakes; D013917:Thrombin / Q000302:isolation & purification* / Q000502:physiology
chemical_list: D003435:Crotalid Venoms; D005340:Fibrinogen; D013917:Thrombin