Heparinase activity in rat liver

Bradley Arbogast, John J. Hopwood, Albert Dorfman

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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.

LanguageEnglish
Pages610-617
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume75
Issue number3
DOIs
Publication statusPublished - 11 Apr 1977

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Arbogast, Bradley ; Hopwood, John J. ; Dorfman, Albert. / Heparinase activity in rat liver. In: Biochemical and Biophysical Research Communications. 1977 ; Vol. 75, No. 3. pp. 610-617.
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Heparinase activity in rat liver. / Arbogast, Bradley; Hopwood, John J.; Dorfman, Albert.

In: Biochemical and Biophysical Research Communications, Vol. 75, No. 3, 11.04.1977, p. 610-617.

Research output: Contribution to journalArticle

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