Y. Jin et al., Purification and characterization of jerdofibrase, a serine protease from the venom of Trimeresurus jerdonii snake, TOXICON, 39(8), 2001, pp. 1203-1210
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.