Characterization of Habu thrombin-like enzyme (THLE) with a new n-terminal sequence from the venom of Trimeresurus flavoviridis (Habu).
A thrombin-like enzyme with a new amino-terminal sequence was isolated from the venom of Trimeresurus flavoviridis using Q-Sepharose, CM-Cellulose, and HW55 column chromatographies. Homogeneity was confirmed by the formation of a single band in polyacrylamide gel electrophoresis. The enzyme has a molecular weight of 29,000 Da. This thrombin-like enzyme was inhibited by p-amidinophenylmethanesulfonyl fluoride hydrochloride (p-APMSF), and dithiothreitol (DTT) suggesting that serines and disulfide bonds are involved in the expression of the enzyme's clotting activity. This thrombin-like enzyme hydrolyzes the Aalpha-chain and Bbeta-chain of bovine fibrinogen. The enzyme was stable to heat treatment.
Komori
Yumiko
Y
Department of Microbiology, Faculty of Pharmacy, Meijo University, Yagotoyama, Nagoya, Japan.
Tanaka
Kikuyo
K
Nikai
Toshiaki
T
D000818:Animals; D002417:Cattle; D003435:Crotalid Venoms / Q000737:chemistry / Q000201:enzymology* / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen / Q000378:metabolism; D006868:Hydrolysis; D013917:Thrombin / Q000819:agonists; D017841:Trimeresurus
D003435:Crotalid Venoms; C029748:Trimeresurus venoms; D005340:Fibrinogen; D013917:Thrombin