Premium
PURIFICATION AND IMMUNOHISTOCHEMICAL LOCALIZATION OF RAT BRAIN MYELIN PROTEOLIPID PROTEIN 1
Author(s) -
Agrawal H. C.,
Hartman B. K.,
Shearer W. T.,
Kalmbach S.,
Margolis F. L.
Publication year - 1977
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.1471-4159.1977.tb10420.x
Subject(s) - myelin , proteolipid protein 1 , antiserum , biochemistry , myelin proteolipid protein , biology , myelin basic protein , cytoplasm , chemistry , microbiology and biotechnology , antibody , central nervous system , immunology , endocrinology
— A homogeneous preparation of proteolipid protein (PLP) from rat brain myelin was isolated by preparative gel electrophoresis in sodium dodecyl sulfate and chemically characterized. The results of amino acid and N ‐terminal amino acid analyses are reported. The same preparation of myelin PLP was used to produce specific precipitating antibodies. Rabbit and goat antisera to myelin PLP each gave a single precipitin line with purified PLP dissolved in Triton X‐100. Under identical conditions, no precipitation was observed with antiserum to myelin basic protein or with control serum. Immunofluorescence localization employing antiserum to PLP demonstrated bright specific fluorescence restricted to the myelin sheaths of axons in all anatomical areas of the rat brain examined. Neuronal cell bodies and their dendrites were completely negative with respect to the presence of proteolipid protein. PLP could not be localized in the cell bodies or fibrous processes in any of the glial elements in the adult rat brain. However, myelin PLP was clearly visible in the cytoplasm and processes of actively myelinating oligodendrocytes in the corpus callosum in the brains of 10‐day‐old rats.