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.
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