A novel heparan sulphate with high degree of N-sulphation and high heparincofactor-II activity from the brine shrimp Artemia franciscana

With the aid of heparinase and heparitinases from Flavobacterium heparinum and C-13 and H-I NMR spectroscopy it was shown that the heparan sulphate is olated from the brine shrimp Artemia franciscana exhibits structural featur es intermediate between those of mammalian heparins and heparan sulphates. These include an unusually high degree of N-sulphation with corresponding v ery low degree of N-acetylation), a relatively high content of iduronic aci d residues (both unsulphated and 2-O-sulphated) and a relatively low degree of 6-O-sulphation of the glucosamine residues. The major sequences (glucur onic acid-->N-sulphated glucosamine and glucuronic acid--> N,6-disulphated glucosamine) are most probably arranged in blocks. Although exhibiting negl igible anticlotting activity in the APTT and anti-factor Xa assays the A. f ranciscana heparan sulphate has a high heparin cofactor-II activity (about 1/3 that of heparin). (C) 2000 Elsevier Science B.V. All rights reserved.