Isolation and characterization of a new clotting factor from Bothrops jararacussu (jararacuçu) venom

• Published in: Toxicon (Oxford) Vol. 35; no. 7; pp. 1043 - 1052
• Main Authors: Andrião-Escarso, S.H., Sampaio, S.V., Cunha, O.A.B., Marangoni, S., Oliveira, B., Giglio, J.R.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.07.1997; Elsevier Science
• Subjects: Amino Acids - analysis; Animal poisons toxicology. Antivenoms; Animals; Biological and medical sciences; Blood Coagulation Factors - chemistry; Blood Coagulation Factors - isolation & purification; Bothrops; Bothrops jararacussu; Chromatography, Gel; Crotalid Venoms - chemistry; Fibrin Tissue Adhesive - metabolism; Medical sciences; Thrombin - isolation & purification; Toxicology; Characterization; Vertebrata; Purification; Enzyme; Venom; Animal origin; Isolation; Reptilia; Coagulation factor; Ophidia
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/S0041-0101(96)00222-X

A detailed procedure for the isolation of a new clotting enzyme from the venom of Bothrops jararacussu (common name jararacuçu) is described. The estimated mol. wt of the native protein was 30,100 but 37,500 after reduction by dithiothreitol. Two major close bands corresponding to p I 5.18 and 5.20 were detected by electrofocusing but, after methanolysis, a single band focused at p I 8.20. The mol. wt of the protein moiety of this glycoprotein was 28,500, showing V-V-G-A-D-N-C-N-F-N… as N-terminal sequence. The content of neutral sugar was 4.8% and that of total sugars 5.3%. This clotting factor degraded only the Aα-chain of the fibrinogen molecule. The stability of the clot, when produced in the presence of aprotinin, opens new uses for snake clotting enzymes in the production of fibrin glue.