Abstract
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 language | English (US) |
|---|---|
| Pages (from-to) | 1422-1428 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 67 |
| Issue number | 4 |
| DOIs | |
| State | Published - Dec 15 1975 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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