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
Publication 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.
Source
J Biol Chem. 1994 Apr 22;269(16):11729-33.
Journal/Book/Conference Title
The Journal of biological chemistry
Related Resources
PubMed ID
8163470
Repository Citation
Mandon, Elisabet C.; Kempner, Ellis S.; Ishihara, Masayuki; and Hirschberg, Carlos B., "A monomeric protein in the Golgi membrane catalyzes both N-deacetylation and N-sulfation of heparan sulfate" (1994). Open Access Articles. 821.
https://escholarship.umassmed.edu/oapubs/821