Heparinase activity in rat liver

Bradley Arbogast, John J. Hopwood, Albert Dorfman

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Heparin was degraded to oligosaccharides by an endoglycosidase present in rat liver lysosomes. Inorganic sulfate equivalent to approximately one sulfamide bond cleaved per heparin chain was also released in incubations of N-[35S]heparin with crude lysosomal preparations. There was no evidence of exoglycosidase or further sulfamidase activity although oligosaccharides approaching the size of tetrasaccharide were produced. The endoglycosidase has a broad pH-dependence with optimum activity observed at pH 4.4 and intermediate activity at pH 5.5 and 3.8.

Original languageEnglish
Pages (from-to)610-617
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 11 Apr 1977

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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