title: Purification and characterization of jerdofibrase, a serine protease from the venom of Trimeresurus jerdonii snake.
abstract: 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.
authors: Department of Animal Toxinology, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, Yunnan, China.
authors: Y
authors: Y
authors: Jin
authors: Q M
authors: QM
authors: Lu
authors: J F
authors: JF
authors: Wei
authors: D S
authors: DS
authors: Li
authors: W Y
authors: WY
authors: Wang
authors: Y L
authors: YL
authors: Xiong
mesh_terms: 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
chemical_list: D003435:Crotalid Venoms; D015842:Serine Proteinase Inhibitors; D005337:Fibrin; D005340:Fibrinogen; D012697:Serine Endopeptidases