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CHARACTERIZATION OF THE FRACTION OBTAINED FROM THE CNS OF JIMPY MICE BY A PROCEDURE FOR MYELIN ISOLATION
Author(s) -
Matthieu JeanMarie,
Quarles R. H.,
Webster H. de F.,
Hogan E. L.,
Brady R. O.
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.tb06054.x
Subject(s) - myelin , fraction (chemistry) , glycoprotein , biochemistry , myelin associated glycoprotein , chemistry , proteolipid protein 1 , biology , central nervous system , myelin basic protein , endocrinology , chromatography
— A subcellular fraction (called the 0·85‐fraction) was isolated from the brains of Jimpy mice by a procedure for obtaining myelin of high purity from immature normal brains. The yield of this fraction obtained from 17‐day‐old Jimpy mice was only 5 per cent of that from age matched controls. In the electron microscope, the O·85‐fractions obtained from 9‐ and 17‐day‐old control mice showed many multilayered whorls of myelin, whereas the corresponding fraction from the Jimpy mice was free of multilayered structures which could be recognized as myelin. Basic proteins, proteolipid protein and galactocerebrosides could not be detected in the 0·85‐fraction from Jimpy mice although they were major components of the 0·85‐fractions from both 9‐ and 17‐day‐old control mice. The specific activity of 2′,3′‐cyclic nucleotide 3′‐ phosphohydrolase in the Jimpy 0·85‐fraction was only 15 per cent of the value for controls. These results can be explained either by the 0·85‐fraction from Jimpy brain being a very abnormal ‘myelin’ or by its being primarily non‐myelin contaminants. Little or none of the major glycoprotein found in normal myelin fractions was found in the 0·85‐fraction from Jimpy brains. This finding is strong evidence indicating that the glycoprotein is closely associated with normal myelin in situ.