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 identified and purified to SDS-polyacrylamide gel electrophoresis homogeneity. It is a single chain polypeptide with a molecular weight of 32kDa under reduced condition and 28kDa under non-reduced condition, respectively. The venom protease catalysed the hydrolysis of some chromogenic substrates such as S2238, S2160, S2302 and S2251. It degraded Bbeta-chain of human fibrinogen preferentially. Also the enzyme degraded fibrin directly. Its enzymatic 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 other snake venom serine proteases.
Jin
Y
Y
Department of Animal Toxinology, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, Yunnan, China.
Lu
Q M
QM
Wei
J F
JF
Li
D S
DS
Wang
W Y
WY
Xiong
Y L
YL
D000595:Amino Acid Sequence; D000818:Animals; D003435:Crotalid Venoms / Q000737:chemistry*; D005337:Fibrin / Q000378:metabolism; D005340:Fibrinogen / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D011817:Rabbits; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology
D003435:Crotalid Venoms; D015842:Serine Proteinase Inhibitors; D005337:Fibrin; D005340:Fibrinogen; D012697:Serine Endopeptidases