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Isoforms of a highly specific B beta-chain fibrinogenase from the venom of Crotalus atrox: preliminary observations
H Pirkle1, A Henschen, I Theodor
1Department of Pathology, Medical Sciences I, University of California, Irvine 92717.
Abstract:
Three variants of a Crotalus atrox venom enzyme that cleaves primarily the Arg42 - Ala bond of the B beta-chain of human fibrinogen were separated by high-performance liquid chromatography and were shown by N-terminal sequence analysis to be amino acid isoforms. All are single-chain glycoproteins whose approximate molecular weights lie between 26,000 and 28,000. The isoenzymes also cleaved the A alpha-chain at Arg491 - His, though much more weakly, with strengths for both bonds that varied among the isoforms.