A novel high molecular weight fibrinogenase from the venom of Bitis arietans

A fibrinogenase (Ba 100) with an apparent molecular mass of 100 kDa under n on-reducing conditions and a pI of 5.4 was purified from the venom of the A frican puff adder (Bitis arietans) by fibrinogen affinity chromatography. U nder reducing conditions the protease dissociates into subunits of 21 kDa a nd 16 kDa. N-Terminal amino acid sequencing showed these two chains to have 66.7% homology and homology to C-type lectins. The fibrinogenase activity of Ba100 cleaves the A alpha and B beta chain of fibrinogen rendering the m olecule unable to polymerise into fibrin clots. Ba100 inhibited platelet ag gregation in platelet rich plasma, and clot formation in whole blood, in a concentration dependent manner, (C) 1999 Published by Elsevier Science B.V. All rights reserved.