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Cerebroside Sulfotransferase in Golgi‐Enriched Fractions from Rat Brain
Author(s) -
Benjamins Joyce A.,
Hadden Timothy,
Skoff Robert P.
Publication year - 1982
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1982.tb10875.x
Subject(s) - cerebroside , golgi apparatus , myelin , galactocerebroside , biochemistry , membrane , glucocerebroside , chemistry , microsome , fucose , isopycnic , glycoprotein , biology , endoplasmic reticulum , enzyme , oligodendrocyte , centrifugation , central nervous system , glucocerebrosidase , neuroscience
Golgi‐enriched fractions were prepared from brainstems of 17‐day‐old rats by first floating off myelin, then fractionating the remaining pellet by a series of differential and density gradient centrifugations in sucrose. Fractions enriched in Golgi membranes were recovered at 0.46/0.76 m and 0.76/0.87 m interfaces on the final sucrose gradient as indicated by morphology and the biochemical markers thiamine pyrophosphatase and [ 3 H]fucose‐labeled glycoprotein. Morphology of the two fractions indicated very little contamination with myelin lamellae; however, the presence of significant levels of 2′, 3′‐cyclic nucleotidase in the lighter fraction suggested a contribution from oligodendroglial or myelin‐related membranes. Cerebroside sulfotransferase was highly enriched in the lighter Golgi‐enriched fraction relative to the denser fraction, the post‐34, 880 x g microsomes, and the myelin‐like fraction. In contrast, ceramide galactosyl transferase was more evenly distributed among the fractions. Our results show a more highly localized distribution of sulfatide synthesis than of galactocerebroside synthesis, probably in Golgi membranes or oligodendroglia‐related membranes with similar properties.