Sulfation of Sugar Nucleotides
II. A PARTICULATE SULFOTRANSFERASE SYSTEM CATALYZING THE SULFATION OF URIDINE DIPHOSPHATE N-ACETYLGALACTOSAMINE
Abstract
A sulfotransferase system that catalyzed the sulfation of UDP-N-acetylgalactosamine in the presence of 3'-phosphoadenosine-5'-phosphosulfate was obtained in a particulate form from the isthmus of hen oviduct. The product of sulfation was identified as UDP-N-acetylgalactosamine-4-sulfate, the same compound that accumulates in the isthmus region during egg formation.
Several attempts were made to solubilize the enzyme system following some of the procedures which were successful in solubilizing sulfotransferases for mucopolysaccharide sulfation. No indication was obtained, however, that the enzyme system which produces UDP-N-acetylgalactosamine-4-sulfate could be solubilized.
Results from examination for substrate specificity and from kinetic studies indicated that the synthesis of UDP-N-acetylgalactosamine-4-sulfate is the principal function of this enzyme system. This was also supported by the finding that the enzyme system tends to be much lower in content in the adjacent magnum region (synonym: albumin-secreting region) where UDP-N-acetylgalactosamine-4-sulfate does not accumulate in more than trace amounts.
Footnotes
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- Received June 17, 1970.
- © 1970, by the American Society of Biological Chemists, Inc.
