Substrate Specificity of a Heparan Sulfate-Degrading Endoglucuronidase from Human Placenta
- 1 January 1979
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 360 (2) , 1465-1472
- https://doi.org/10.1515/bchm2.1979.360.2.1465
Abstract
A heparan sulfate-degrading endoglucuronidase was isolated from human placenta and partially purified by affinity chromatography on heparan sulfate-Sepharose 4B. The endoglucuronidase has a MW of .apprx. 100,000 estimated by gel chromatography and a broad pH optimum between pH4-pH6. Carboxyl reduced heparan sulfate is not split by partially purified endoglucuronidase, but inhibits the action of that enzyme towards non-modified heparan sulfate. Low MW heparan sulfate (MW .apprxeq. 3000) is not attacked by the endoglucuronidase. N-Desulfated heparan sulfate and heparin are only weak substrates. The amino sugar adjacent to the glucuronic acid residue appearing at the reducing terminal of heparan sulfate fragments liberated by the endoglucuronidase appears to be exclusively N-acetylated glucosamine.This publication has 5 references indexed in Scilit:
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