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Depolarizing Agents Regulate the Phosphorylation of Myelin Basic Protein in Rat Optic Nerves
Author(s) -
Murray Norman,
Steck Andreas J.
Publication year - 1983
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.1471-4159.1983.tb04773.x
Subject(s) - phosphorylation , myelin basic protein , myelin , protein phosphorylation , depolarization , in vitro , endogeny , microbiology and biotechnology , chemistry , calcium , chlorpromazine , biochemistry , biology , neuroscience , biophysics , central nervous system , pharmacology , protein kinase a , organic chemistry
The regulation of the state of phosphorylation of myelin basic protein has been studied in intact rat optic nerves incubated in vitro . For this purpose the endogenous state of phosphorylation was preserved and the “back‐phosphorylation” technique was used to determine the amount of dephosphorylated protein present in extracts of the nerves. Our results indicate that when nerves were incubated in the presence of depolarizing agents, the state of phosphorylation of myelin basic protein was increased. This effect was calcium‐dependent and was partly inhibited by chlorpromazine.