Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0003-9861(02)00447-2
Title: A novel prothrombin activator from the venom of Micropechis ikaheka: Isolation and characterization
Authors: Gao, R.
Gopalakrishnakone, P. 
Kini, R.M. 
Keywords: Disintegrin
Elapid
Metalloproteinase
Prothrombin activator
Snake venom
Issue Date: 2002
Source: Gao, R., Gopalakrishnakone, P., Kini, R.M. (2002). A novel prothrombin activator from the venom of Micropechis ikaheka: Isolation and characterization. Archives of Biochemistry and Biophysics 408 (1) : 87-92. ScholarBank@NUS Repository. https://doi.org/10.1016/S0003-9861(02)00447-2
Abstract: A novel prothrombin activator, Mikarin, has been isolated from Micropechis ikaheka venom. It is a single polypeptide chain metalloproteinase with the apparent molecular weight of 47 kDa. Mikarin exhibits Ca2+-independent prothrombin activation, but no effects on other blood coagulation factors, such as factor X and fibrinogen. Mikarin is the first member of group I prothrombin activators from elapid venom. Like other high-molecular-weight snake venom proteinases, it has three structural domains, metalloproteinase and disintegrin-like and Cys-rich domains, and belongs to the P-III class of snake venom metalloproteinases. The N-terminal of Mikarin exhibits 76% sequence identity with Cobrin, a metalloproteinase identified from Naja naja venom, but very lower identities were found when compared with those from viperid and crotalid venom. In addition, the presence of disintegrin-like and Cys-rich domains in snake venom metalloproteinases with diverse biological activities suggests that these domains may be important for their function. © 2002 Elsevier Science Ltd. All rights reserved.
Source Title: Archives of Biochemistry and Biophysics
URI: http://scholarbank.nus.edu.sg/handle/10635/33904
ISSN: 00039861
DOI: 10.1016/S0003-9861(02)00447-2
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