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The Journal of Cell Biology, Vol 99, 327-331, Copyright © 1984 by The Rockefeller University Press

ARTICLES

Two enzymes involved in the synthesis of O-linked oligosaccharides are localized on membranes of different densities in mouse lymphoma BW5147 cells

A Elhammer and S Kornfeld

Microsomal membranes from mouse lymphoma BW5147 cells were fractionated on a continuous sucrose gradient and assayed for two enzymes involved in the synthesis of O-linked oligosaccharides. Both enzymes were recovered in membranes that were less dense than the membranes containing the endoplasmic reticulum marker enzymes, glucosidase I and II. UDP-Gal:N-acetylgalactosamine-beta 1, 3-galactosyltransferase had a distribution that coincided with that of the galactosyltransferase that acts on asparagine-linked oligosaccharides. This latter enzyme has been immunolocalized to the trans Golgi elements. The UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase was recovered in a membrane fraction of intermediate density, between the endoplasmic reticulum and trans Golgi markers. These findings are consistent with the assembly of O- linked oligosaccharides occurring in at least two different Golgi compartments.
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