Purification and characterization of jerdofibrase, a serine protease from the venom of Trimeresurus jerdonii snake

A fibrin(ogen)olytic serine protease from Trimeresurus jerdonii venom was i dentified and purified to SDS-polyacrylamide gel electrophoresis homogeneit y. It is a single chain polypeptide with a molecular weight of 32 kDa under reduced condition and 28 kDa under non-reduced condition, respectively. Th e venom protease catalysed the hydrolysis of some chromogenic substrates su ch as S2238, S2160, S2302, and S2251. It degraded B beta -chain of human fi brinogen preferentially. Also the enzyme degraded fibrin directly. Its enzy matic activity was. completely inhibited by phenylmethylsulfonyl fluoride ( PMSF). but not affected by EDTA. That suggested it was a serine protease. N -terminal sequence of the purified component showed high homology with othe r snake venom serine proteases. (C) 2001 Elsevier Science Ltd. All rights r eserved.