Identification and Characterization of a Thrombin-like enzyme isolated from Deinagkistrodon acutus venom
A thrombin-like enzyme was isolated from Deinagkistrodon acutus venom by a combination of affinity and ion exchange chromatography. The enzyme presented ~40 kD by reducing SDS-PAGE analysis, ~34 kD by MALDI-TOF-TOF-MS analysis, and was shown to be glycosylated with ~6 kD O-linked carbohydrates, with pI ~4.8±0.2. The enzyme had optimal esterase activity on BAEE and the most serious degradation at pH 9, displayed maximum catalytic rate at ~50. Its hydrolytic activity was ℃ inhabited by Aprotinin, PMSF, AEBSF and Benzamidine. The enzyme also showed fibrinogen (Fg) clotting activity and amidase activity on DL-BAPA. N-terminal 15 amino acid sequence, PMF analysis and amino acid combination analysis revealed that it has high similarity with other thrombin like enzymes from snake venoms.
enzymatic characterization thrombin-like enzyme deinagkistrodon
Yu Xi Dexian Dong Rongxiu Li
MOE Key Laboratory of Microbial Metabolism, College of Life Science and biotechnology, Shanghai Jiao tong University, 800 Dongchuan Road, Shanghai 200240, China
国际会议
The 5th International Conference on Separation Science and Technology(第五届国际分离科学与技术会议)
北京
英文
2007-10-14（万方平台首次上网日期，不代表论文的发表时间）