Abstract
A membrane-associated galactosyltransferase has been purified to homogeneity from the fission yeast, Schizosaccharomyces pombe. The enzyme has a molecular weight of 61,000 and is capable of transfering galactose from UDP-galactose (UDP-Gal) to a variety of mannose-based acceptors to form an alpha-1,2 galactosyl mannoside linkage. Immunofluorescence localization of the protein is consistent with the presence of the enzyme in the Golgi apparatus of S. pombe. This, together with the presence of terminal, alpha-linked galactose on the N-linked oligosaccharides of S. pombe secretory proteins, suggests that the galactosyltransferase is an enzyme involved in the processing of glycoproteins transported through the Golgi apparatus in fission yeast.
MeSH Terms
Chromatography, Affinity
Chromatography, Gel
Chromatography, Ion Exchange
Cytosol/enzymology
Edetic Acid/pharmacology
Fluorescent Antibody Technique
Galactosyltransferases/isolation & purification,metabolism
Glycoproteins/genetics
Golgi Apparatus/enzymology,ultrastructure
Histocytochemistry
Kinetics
Manganese/pharmacology
Microsomes/enzymology
Molecular Weight
Protein Processing, Post-Translational
Saccharomycetales/enzymology
Schizosaccharomyces/enzymology,ultrastructure
Substrate Specificity
Chemicals
Glycoproteins
Manganese
Edetic Acid
Galactosyltransferases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Chappell T G
Imperial Cancer Research Fund, London, United Kingdom.
Warren G
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