A heparan sulfate-degrading endoglycosidase from rat liver tissue. Academic Article

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. 1975.

authors

• Hook, Magnus

published proceedings

• Biochem Biophys Res Commun

altmetric score

• 6

author list (cited authors)

• Hk, M., Wasteson, A., & Oldberg, A.

citation count

• 84

complete list of authors

• Höök, M||Wasteson, A||Oldberg, A

publication date

• January 1975

publisher

• Elsevier  Publisher

published in

• Biochemical and Biophysical Research Communications  Journal

keywords

• Animals
• Cell Line
• Glycosaminoglycans
• Glycoside Hydrolases
• Heparitin Sulfate
• Hydrogen-Ion Concentration
• Liver
• Lysosomes
• Male
• Rats

Digital Object Identifier (DOI)

• 10.1016/0006-291x(75)90185-0

start page

• 1422

end page

• 1428

volume

• 67

issue

• 4

URL

• http://dx.doi.org/10.1016/0006-291x(75)90185-0