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

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Document Type



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


Life Sciences | Medicine and Health Sciences


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.


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

Journal/Book/Conference Title

The Journal of biological chemistry

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