Biochemical characterization of a thrombin-like enzyme and a fibrinolytic serine protease from snake (Agkistrodon saxatilis) venom

Citation
Ys. Koh et al., Biochemical characterization of a thrombin-like enzyme and a fibrinolytic serine protease from snake (Agkistrodon saxatilis) venom, TOXICON, 39(4), 2001, pp. 555-560
Citations number
14
Categorie Soggetti
Pharmacology & Toxicology
Journal title
TOXICON
ISSN journal
00410101 → ACNP
Volume
39
Issue
4
Year of publication
2001
Pages
555 - 560
Database
ISI
SICI code
0041-0101(200104)39:4<555:BCOATE>2.0.ZU;2-5
Abstract
A thrombin-like enzyme and a fibrinolytic serine protease were purified to homogeneity from the venom of a Korean snake Agkistrodon saxatilis emeliano v. Both the purified enzymes migrated as a single protein band correspondin g to 39 kDa in SDS-PAGE. However, the molecular mass was reduced to 28 kDa by enzymatic removal of the N-linked carbohydrates in those two different e nzyme species. Although the thrombin-like enzyme and the fibrinolytic prote ase show homologous features in their molecular sizes and N-terminal amino acid sequences, yet they can be clearly distinguished from each other in te rms of substrate specificity, susceptibility to inhibitors and fibrinogen d egradation. It is postulated that these two enzymes are capable of function ing in a cooperative manner to effectively remove fibrinogen and consequent ly to reduce the blood viscosity. (C) 2000 Elsevier Science Ltd. All rights reserved.