A novel serine protease from the snake venom of Agkistrodon blomhoffii ussurensis.

ABSTRACT: A novel serine protease, ABUSV-SPase, was isolated to homogeneity for the first time from Chinese Agkistrodon blomhoffii ussurensis snake venom, and its enzymatic and structural properties were characterized by multiple techniques. ABUSV-SPase is a stable monomeric protein with a molecular mass of 26,752.6a.m.u. It reacts optimally with its substrate Nalpha-tosyl-l-arginine methyl ester (TAME) at pH 7.0 and 41 degrees C. ESI-MS/MS analysis indicates that ABUSV-SPase is a new serine protease, sharing peptide homologies with various snake venom serine proteases, especially the snake venom thrombin-like enzymes of this group, and serine protease precursors. It is a zinc-containing protein, and although zinc is not essential for activity, its replacement by various divalent metal ions, includi

SUBMITTER: Liu S 

PROVIDER: S-EPMC2845635 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature