Agkihpin, a novel SVTLE from Gloydius halys Pallas, promotes platelet aggregation in vitro and inhibits thrombus formation in vivo in murine models of thrombosis.

摘要: Abstract In previous work, a snake venom arginine esterase (SVAE), agkihpin from the of Gloydius halys Pallas, was isolated and its biochemical data including Mr, PI, amino acid components sugar content collected. Here, cloned further characterized we found that could promote ADP-induced platelets aggregation, hydrolyze fibrin, cleave Aα Bβ chains fibrinogen reduce thrombosis induced by thrombin. Moreover, hydrolyzed TAME with optimum temperatures at 30 °C–45 °C, hydrolysis inhibited EDTA, PMSF, DTT promoted Ca2+, Fe3+, Mg2+, Zn2+. The sequence features were detected as follows: N-terminal residues determined I(V)L(Y)GDDECNINE protein sequencing; ORF 705 bp, deduced identified peptide mass fingerprinting; cysteines, cleavage sites, active sites substrate binding thrombin-like enzyme (SVTLE), all conserved in agkihpin; 2 Leu(Tyr), 4 Asn 121 Ile first sequences SVTLEs. These findings indicated is novel SVTLE. What's more, due to several advantages fibrino(gen)olytic thrombosis-reduced activities, devoid bleeding risk, may be developed into thrombolytic drug future.