A heparan sulfate-degrading endoglycosidase from rat liver tissue

Magnus Höök, Åke Wasteson, Åke Oldberg

Research output: Contribution to journalArticlepeer-review

69 Scopus citations


Incubation of a rat liver lysosomal fraction with [35S]heparan sulfate resulted in degradation of the polymer to oligosaccharides, demonstrating the presence of a heparan sulfate-degrading endoglycosidase. Judging from the size of the oligosaccharides, representing degradation end-products, only a limited number of the glycosidic linkages in the heparan sulfate molecule would seem to be susceptible to the heparitinase. The pH-dependence of the enzyme (active at pH 5.6; inactive at pH 3.8) was found to differ from that of liver hyaluronidase (active at pH 3.8; inactive at pH 5.6), suggesting that the heparitinase is a previously unknown enzyme.

Original languageEnglish (US)
Pages (from-to)1422-1428
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Dec 15 1975

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'A heparan sulfate-degrading endoglycosidase from rat liver tissue'. Together they form a unique fingerprint.

Cite this