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ANOMALIES OF MYELIN‐ASSOCIATED GLYCOPROTEINS IN‘QUAKING MICE
Author(s) -
Matthieu JeanMarie,
Brady R. O.,
Quarles R. H.
Publication year - 1974
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.1471-4159.1974.tb11592.x
Subject(s) - myelin , glycoprotein , myelin associated glycoprotein , fucose , biochemistry , gel electrophoresis , proteolipid protein 1 , mutant , polyacrylamide gel electrophoresis , biology , microbiology and biotechnology , chemistry , myelin basic protein , central nervous system , endocrinology , enzyme , gene
— Proteins and glycoproteins in a myelin fraction isolated from Quaking mutant mice were separated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate and stained with Fast Green or with periodic acid‐Schiff reagents. Double labelling experiments with [ 3 H]fucose and [ 14 C]fucose were also used to compare glycoproteins in myelin from the mutant mice with those from control mice. In the myelin fraction from the Quaking mice the basic proteins and proteolipid protein were decreased relative to the high molecular weight proteins. Some glycoproteins which are present in small amounts in myelin from normal mice were increased relative to the major glycoprotein in the myelin fraction of the Quaking mice. Furthermore, the major myelin‐associated glycoprotein was shifted toward higher apparent molecular weight in comparison with controls of the same age or even with 9‐day‐old controls. The abnormal glycoproteins in the mutant myelin fraction could be a factor in the impairment of myelination.