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

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-deacetyla...

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Bibliographic Details
Published in:The Journal of biological chemistry 1994-04, Vol.269 (16), p.11729-11733
Main Authors: MANDON, E, KEMPNER, E. S, ISHIHARA, M, HIRSCHBERG, C. B
Format: Article
Language:English
Subjects:
Amidohydrolases - chemistry
Amidohydrolases - metabolism
Amidohydrolases - radiation effects
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Dose-Response Relationship, Radiation
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Golgi Apparatus - metabolism
Golgi Apparatus - radiation effects
Heparitin Sulfate - metabolism
Intracellular Membranes - metabolism
Intracellular Membranes - radiation effects
Kinetics
Liver - metabolism
Molecular Weight
Rats
Sulfotransferases - chemistry
Sulfotransferases - metabolism
Sulfotransferases - radiation effects
Transferases
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)32633-9