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.
| Language | English |
|---|---|
| Pages | 610-617 |
| Number of pages | 8 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 75 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 11 Apr 1977 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
}
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 journal › Article
TY - JOUR
T1 - Heparinase activity in rat liver
AU - Arbogast, Bradley
AU - Hopwood, John J.
AU - Dorfman, Albert
PY - 1977/4/11
Y1 - 1977/4/11
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.
UR - http://www.scopus.com/inward/record.url?scp=0017338888&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(77)91516-9
DO - 10.1016/0006-291X(77)91516-9
M3 - Article
VL - 75
SP - 610
EP - 617
JO - Biochemical and Biophysical Research Communications
T2 - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -