Journal article
Batroxobin Binds Fibrin with Higher Affinity and Promotes Clot Expansion to a Greater Extent than Thrombin*
Abstract
Batroxobin is a thrombin-like serine protease from the venom of Bothrops atrox moojeni that clots fibrinogen. In contrast to thrombin, which releases fibrinopeptide A and B from the NH2-terminal domains of the Aα- and Bβ-chains of fibrinogen, respectively, batroxobin only releases fibrinopeptide A. Because the mechanism responsible for these differences is unknown, we compared the interactions of batroxobin and thrombin with the predominant …
Authors
Vu TT; Stafford AR; Leslie BA; Kim PY; Fredenburgh JC; Weitz JI
Journal
Journal of Biological Chemistry, Vol. 288, No. 23, pp. 16862–16871
Publisher
Elsevier
Publication Date
June 2013
DOI
10.1074/jbc.m113.464750
ISSN
0021-9258