Characterization of a Platelet Endoglycosidase Degrading Heparin-like Polysaccharides

Åke Oldberg, Magnus Höök, Carl Henrik Heldin, Åke Wasteson, Christer Busch

Research output: Contribution to journalArticlepeer-review

82 Scopus citations


An endoglycosidase (heparitinase) acting on heparin and heparan sulfate was partially purified (∼300 times) from human platelets by affinity chromatography on heparan sulfate substituted Sepharose. Only heparin-like polysaccharides were degraded by the enzyme. The susceptibility of various biosynthetic heparin intermediates indicated that the platelet heparitinase had a requirement for sulfamino but not ester sulfate groups. No activity toward other uronic acid containing glycosaminoglycans could be demonstrated. Glucuronidic but not glucosaminidic linkages in heparin or heparan sulfate were attacked by the enzyme as shown by analysis of the reducing sugar moiety in oligosaccharide products. The anticoagulant activity of heparin, determined in an antithrombin III activation assay, was markedly reduced after treatment with the heparitinase. The enzyme was released from its storage site in platelets after induction of the platelet release reaction. The physiological function of platelet heparitinase is not known but may be to modify extracellular heparin-like polysaccharides in the vascular system.

Original languageEnglish (US)
Pages (from-to)5755-5762
Number of pages8
Issue number25
StatePublished - Feb 1 1980

ASJC Scopus subject areas

  • Biochemistry


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