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FRACTIONATION OF SOLUBLE BRAIN GLYCOPROTEINS BY AFFINITY AND HYDROXYLAPATITE CHROMATOGRAPHY
Author(s) -
Langley O. K.
Publication year - 1979
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.1471-4159.1979.tb11724.x
Subject(s) - hydroxylapatite , glycoprotein , fucose , chromatography , chemistry , gel electrophoresis , fractionation , polyacrylamide gel electrophoresis , biochemistry , affinity chromatography , enzyme
—A separation of soluble brain proteins and Con A‐binding glycoproteins by chromatography on calcium hydroxylapatite in the presence of SDS is described. Seventeen Coomassie Blue‐stained bands were detected by polyacrylamide gel electrophoresis in SDS of Con A‐binding glycoproteins of the soluble fraction of rat brain: 16 of these were found by in vivo uptake of [ 3 H]fucose to be fucosylglycoproteins. Hydroxylapatite chromatography yielded several glycoprotein pools, each of which was shown by gel electrophoresis to contain between 4 and 8 individual glycoproteins. Such pools were enriched in [ 36 H]fucose relative to the brain soluble fraction by factors of between 6 and 21. Preliminary experiments demonstrate that this method is also applicable to the fractionation of membrane‐bound glycoproteins.