title: Determination of the range in binding-site densities of rat skin heparin chains with high binding affinities for antithrombin.
abstract: Rat skin heparin proteoglycans vary markedly in the proportions of their constituent polysaccharide chains that have high binding affinity for antithrombin. As the proportion of such chains in a proteoglycan rises, their degree of affinity for antithrombin also increases [Horner (1987) Biochem. J. 244, 693-698]. The antithrombin-binding-site densities of such chains have now been determined, by measuring heparin-induced enhancement of the intrinsic fluorescence of antithrombin and by chemical analysis for the disaccharide sequence glucuronosyl-N-sulphoglucosaminyl (3,6-di-O-sulphate), which is unique to this site in heparin [Lindahl, Bäckström, Thunberg & Leder (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 6551-6555]. Antithrombin-binding-site density ranged from one to five sites per chain.
authors.affiliation: Department of Physiology, University of Toronto, Ont., Canada.
authors.forename: A A
authors.initials: AA
authors.lastname: Horner
authors.forename: M
authors.initials: M
authors.lastname: Kusche
authors.forename: U
authors.initials: U
authors.lastname: Lindahl
authors.forename: C B
authors.initials: CB
authors.lastname: Peterson
mesh_terms: D000818:Animals; D000991:Antithrombins / Q000378:metabolism*; D001665:Binding Sites; D006493:Heparin / Q000378:metabolism*; D011485:Protein Binding; D011509:Proteoglycans / Q000378:metabolism; D051381:Rats; D012867:Skin / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
chemical_list: D000991:Antithrombins; D011509:Proteoglycans; D006493:Heparin