Structural features and anticoagulant activities of a novel natural low molecular weight heparin from the shrimp Penaeus brasiliensis

A natural low molecular weight heparin (8.5 kDa), with an anticoagulant activity of 95 IU/mg by the USP assay, was isolated from the shrimp Penaeus brasiliensis. the crustacean heparin was susceptible to both heparinase and heparitinase II from Flavobacterium heparinum forming tri- and di-sulfated disaccharides as the mammalian heparins. C-13 and H-1 NMR spectroscopy revealed that the shrimp heparin was enriched in both glucuronic and non-sulfated iduronic acid residues. the in vitro anticlotting activities in different steps of the coagulation cascade have shown that its anticoagulant action is mainly exerted through the inhibition of factor Xa and heparin cofactor II-mediated inhibition of thrombin. the shrimp heparin has also a potent in vivo antithrombotic activity comparable to the mammalian low molecular weight heparins. (C) 1999 Elsevier Science B.V. All rights reserved.Universidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, BrazilUniv Fed Rio Grande Norte, Dept Bioquim, Natal, RN, BrazilLoyola Med Sch, Dept Pathol, Maywood, IL USAUniv Fed Parana, Dept Bioquim, BR-80060000 Curitiba, Parana, BrazilUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, BrazilWeb of Scienc