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Subcellular site of the biosynthesis ofO-acetylated sialic acids in bovine submandibular gland

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Abstract

Bovine submandibular glands were homogenized and fractionated under conditions which yielded subcellular fragments from mainly one cell type, the mucous acinar cell, as judged by morphological analysis of the glands before and after homogenization. The majorN-acetylneuraminate-9(7)-O-acetyltransferase activity was detected in the cytosolic fraction, a result supported by the high specific radioactivity of free sialic acids isolated after [14C]acetate-labelling experiments. Separation of membranes on a Ficoll density gradient gave six fractions which were analyzed biochemically and morphologically. The particulate activities of acetyltransferase and sialyltransferase were found in fractions containing smooth and mitochondrial membranes. MembraneO-acetyl sialic acids were present at the highest levels in these fractions and also had the highest specific radioactivity after [14C]acetate-labelling experiments. Significant amounts of theO-acetyltransferase activity also occur in the cytosol and are consistent with a model ofO-acetyl sialic acid biosynthesis involving both cytosolic and smooth membrane sites ofO-acetylation.

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Authors and Affiliations

  1. Biochemisches Institut, Christian-Albrechts-Universität, Olshausenstr. 40, D-2300, Kiel, Federal Republic of Germany

    Roland Schauer

  2. Sertoriusring 295, D-6500, Mainz 21, Federal Republic of Germany

    Jorge Casals-stenzel

  3. Department of Medicine Laboratories, Bristol Royal Infirmary, BS2 8HW, Bristol, UK

    Anthony P Corfield

  4. Institut für Anatomie, Ruhr-Universität, Postfach 102148, D-4630, Bochum 1, Federal Republic of Germany

    Rüdiger W Veh

Authors
  1. Roland Schauer
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  2. Jorge Casals-stenzel
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  3. Anthony P Corfield
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  4. Rüdiger W Veh
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Schauer, R., Casals-stenzel, J., Corfield, A.P. et al. Subcellular site of the biosynthesis ofO-acetylated sialic acids in bovine submandibular gland. Glycoconjugate J 5, 257–270 (1988). https://doi.org/10.1007/BF01049086

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  • DOI: https://doi.org/10.1007/BF01049086

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Enzymes

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