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Identification and characterization of Harobin, a novel fibrino(geno)lytic serine protease from a sea snake ( Lapemis hardwickii )
Author(s) -
He Junyun,
Chen Shiyong,
Gu Jun
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.05.047
Subject(s) - serine protease , kininogen , proteases , in vivo , biochemistry , serine , fibrinogen , snake venom , protease , pichia pastoris , microbiology and biotechnology , elastase , biology , chemistry , recombinant dna , venom , enzyme , kallikrein , gene
Recombinant Harobin exhibits an amidolytic activity, and specifically degrades Aα, Bβ‐chain of fibrinogen. It functions as a defibrase both in vitro and in vivo, and reduces thrombosis. Harobin prolongs the coagulation time and the bleeding time of mice and reduces the fibrinogen levels of rats as well. Meanwhile, intravenous injection of Harobin leads to the reduction of blood pressure in SHR rats. It results from the ability of Harobin that cleaves angiotensin I and release bradykinin from plasma kininogen in vitro and in vivo. These data suggest that Harobin is a novel defibrase and has a potential to be an agent for the therapy of thrombosis and hypertension.