Heparinase activity in rat liver

Bradley Arbogast; John J. Hopwood; Albert Dorfman

doi:10.1016/0006-291X(77)91516-9

Heparinase activity in rat liver

Bradley Arbogast, John J. Hopwood, Albert Dorfman

Hopwood Centre For Neurobiology

Research output: Contribution to journal › Article

5 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.

Original language	English
Pages (from-to)	610-617
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	75
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(77)91516-9
Publication status	Published - 11 Apr 1977

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(77)91516-9

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Cite this

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title = "Heparinase activity in rat liver",

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.",

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AU - Hopwood, John J.

AU - Dorfman, Albert

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N2 - 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.

AB - 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.

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