Jerdonase, a novel serine protease with kinin-releasing and fibrinogenolytic activity from Trimeresurus jerdonii venom.
A novel kinin-releasing and fibrin(ogen)olytic enzyme termed jerdonase was purified to homogeneity from the venom of Trimeresurus jerdonii by DEAE Sephadex A-50 anion exchange, Sephadex G-100 (superfine) gel filtration and reverse-phase high performance liquid chromatography (RP-HPLC). Jerdonase migrated as a single band with an approximate molecular weight of 55 kD under the reduced conditions and 53 kD under the non-reduced conditions. The enzyme was a glycoprotein containing 35.8% neutral carbohydrate. The N-terminal amino acid sequence of jerdonase was determined to be IIGGDECNINEHPFLVALYDA, which showed high sequence identity to other snake venom serine proteases. Jerdonase catalyzed the hydrolysis of BAEE, S-2238 and S-2302, which was inhibited by phenylmethylsulfonyl fluoride (PMSF), but not affected by ethylenediaminetetraacetic acid (EDTA). Jerdonase preferentially cleaved the A alpha-chain of human fibrinogen with lower activity towards B beta-chain. Moreover, the enzyme hydrolyzed bovine low-molecular-mass kininogen and releasing bradykinin. In conclusion, all results indicated that jerdonase was a multifunctional venom serine protease.
Jia
Yong-Hong
YH
Department of Animal Toxicology, Kunming Institute of Zoology, the Chinese Academy of Sciences, Kunming 650223, China. jiayh_78@hotmail.com
Jin
Yang
Y
Lü
Qiu-Min
QM
Li
Dong-Sheng
DS
Wang
Wan-Yu
WY
Xiong
Yu-Liang
YL
D000595:Amino Acid Sequence; D000818:Animals; D002845:Chromatography; D003435:Crotalid Venoms / Q000032:analysis* / Q000302:isolation & purification*; D005340:Fibrinogen / Q000378:metabolism*; D007705:Kinins; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000502:physiology
D003435:Crotalid Venoms; D007705:Kinins; D005340:Fibrinogen; D012697:Serine Endopeptidases; C481204:jerdonase, Trimeresurus jerdonii