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- W2029556483 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 β-chain of fibrinogen and the appearance of lower molecular weight fragments. Thus the enzyme can be classified as a β-fibrinogenase. However, on prolonged incubation of the fibrinogen there was also a partial digestion of the α-chain. The fibrinogenase showed no activity towards fibrin or casein or arginine esters. The fibrinogenolytic activity was inihibited by phenylmethanesulphonyl fluoride (PMSF) but was unaffected by EDTA." @default.
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- W2029556483 date "1983-09-01" @default.
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- W2029556483 title "Purification and characterization of a fibrinogenase from the venom of Western Diamondback rattlesnake (Crotalus atrox)" @default.
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- W2029556483 doi "https://doi.org/10.1016/0167-4838(83)90101-2" @default.
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