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ARE MYELIN PROTEINS SYNTHESIZED IN RETINAL GANGLION CELLS? 1
Author(s) -
Prensky A. L.,
Fujimoto Karen,
Agrawal H. C.
Publication year - 1975
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.1471-4159.1975.tb04422.x
Subject(s) - proteolipid protein 1 , myelin , myelin basic protein , polyacrylamide gel electrophoresis , chemistry , retinal , major basic protein , gel electrophoresis , biochemistry , optic nerve , microbiology and biotechnology , biology , anatomy , central nervous system , endocrinology , immunology , enzyme , eosinophil , asthma
—We studied the incorporation of radioactivity into individual proteins of myelin by sodium dodecyl sulfate polyacrylamide gel electrophoresis after the injection of [ 3 H]tryptophan into the right eye of developing rabbits. We found that the specific activity of basic protein (c.p.m./mg of basic protein) and the specific activity of DM‐20 and proteolipid protein (c.p.m./mg total myelin protein applied to the gel) did not approach the ratio predicted by decussation of the fibres of the rabbit optic nerve. The specific activity of Wolfgram protein, however, approached an expected ratio of 15:1. We therefore concluded that myelin basic protein, DM‐20 and proteolipid protein were probably not synthesized in retinal ganglion cells.