From the venom of Trimeresurus jerdonii, a distinct thrombin-like enzyme, c
alled jerdonobin. was purified by DEAF A-25 ion-exchange chromatography, Se
phadex G-75 gel filtration, and fast protein liquid chromatography (FPLC).
SDS-PAGE analysis of this enzyme shows that it consists of a single polypep
tide chain with a molecular weight of 38,000. The NH2-terminal amino acid s
equence of jerdonobin has great homology with venom thrombin-like enzymes d
ocumented. Jerdonobin is able to hydrolyze several chromogenic substrates.
The enzyme directly clots fibrinogen with an activity of 217 NIH units/mg,
The fibrinopeptides released, identified by HPLC consisted of fibrinopeptid
e A and a small amount of fibrinopepide B. The activities of the enzyme wer
e inhibited by phenylmethylsulfonyl fluoride (PMSF) and p-nitrophenyl-p-gua
nidinobenzoate (NPGB). However, metal chelator (EDTA) had no effect on it.
indicating it is venom serine protease. (C) 2000 Elsevier Science Ltd. All
rights reserved.