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. 2003 Aug;35(8):689-94.

Jerdonase, a Novel Serine Protease With Kinin-Releasing and Fibrinogenolytic Activity From Trimeresurus Jerdonii Venom

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  • PMID: 12897962
Free article

Jerdonase, a Novel Serine Protease With Kinin-Releasing and Fibrinogenolytic Activity From Trimeresurus Jerdonii Venom

Yong-Hong Jia et al. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). .
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Abstract

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.

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