Title

A monomeric protein in the Golgi membrane catalyzes both N-deacetylation and N-sulfation of heparan sulfate

UMMS Affiliation

Department of Biochemistry and Molecular Biology

Date

4-22-1994

Document Type

Article

Subjects

Amidohydrolases; Animals; Dose-Response Relationship, Radiation; Golgi Apparatus; Heparitin Sulfate; Intracellular Membranes; Kinetics; Liver; Molecular Weight; Rats; Sulfotransferases

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

Recent studies have shown that the rat liver heparan sulfate N-deacetylase/N-sulfotransferase is a glycoprotein encoded by a single polypeptide chain of 882 amino acids. Using radiation inactivation analyses, we have now determined that in rat liver Golgi vesicles the target size for the N-deacetylase is 88 +/- 14 kDa, whereas that of the N-sulfotransferase is 92 +/- 8 kDa. These results, together with previous biochemical and molecular cloning approaches, demonstrate that 1) in rat liver Golgi membranes there exists only on population of molecules expressing both activities, 2) the active protein in the Golgi membrane functions as a monomer, and 3) there is no evidence that a large independent protein acts as a regulator of either activity.

Rights and Permissions

Citation: J Biol Chem. 1994 Apr 22;269(16):11729-33.

Related Resources

Link to Article in PubMed

Journal Title

The Journal of biological chemistry

PubMed ID

8163470