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

A detailed procedure for the isolation of a new clotting enzyme from the venom of Bothrops jararacussu (common name jararacucu) 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 pI 5.18 and 5.20 were detected by electrofocusing but, after methanolysis, a single band focused at pI 8.20, The mel. 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 A alpha-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. (C) 1997 Elsevier Science Ltd.