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Isolation of an Endogenous Inhibitor of Ceramide Glycosyltransferases from Rat Brain

  • Elvira Costantino-Ceccarini
  • Alessandro Cestelli
  • Kunihiko Suzuki
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 101)

Abstract

Galactosylceramide is generally considered to be the characteristic constituent of myelin, although recent studies have shown that this lipid is also present in a substantial concentration in myelinated axons freed of myelin (1,2). Reflecting their primary localization in myelin, galactosylceramide biosynthesis shows a peak of activity in developing brain, concomitant with the period of maximal myelin accumulation (3,4). The terminal enzymatic step in the biosynthetic pathway of galactosylceramide is galactosylation of α-hydroxy fatty acid-containing ceramide (HFA-ceramide), catalyzed by UDP-galactose:ceramide galactosyltransferase (E.C. 2.4.1. 62)(5). This enzyme is primarily localized in the microsomal fraction by the conventional subcellular fractionation procedure. However, small proportions of this enzyme are also present in the myelin sheath (6,7) and in an axolemma-enriched fraction (8). The specific activity of the galactosyltransferase in the axolemma fraction is similar to that in the microsomal fraction (8).

Keywords

Microsomal Fraction Endogenous Inhibitor Microsomal Protein Enzyme Source Inhibitor Preparation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • Elvira Costantino-Ceccarini
    • 1
  • Alessandro Cestelli
    • 1
  • Kunihiko Suzuki
    • 1
  1. 1.The Saul R. Korey Department of Neurology, Department of Neuroscience, and the Rose F. Kennedy Center for Research in Mental Retardation and Human DevelopmentAlbert Einstein College of MedicineBronxUSA

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