Isoforms of a highly specific Bbeta;hyphen;chain fibrinogenase from the venom of Crotalus atroxpreliminary observations

摘要

Three variants of aCrotalus atroxvenom enzyme that cleaves primarily the Arg42- Ala bond of the Bbeta;-chain of human fibrinogen were separated by high-performance liquid chromatography and were shown byN-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 Aalpha;-chain at Arg491- His, though much more weakly, with strengths for both bonds that varied among the isoforms