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Effect of Reactive Oxygen Species on Myelin Membrane Proteins
Author(s) -
Konat Gregory W.,
Wiggins Richard C.
Publication year - 1985
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.1471-4159.1985.tb05530.x
Subject(s) - myelin , reactive oxygen species , chemistry , myelin sheath , membrane , biophysics , oxygen , biochemistry , microbiology and biotechnology , neuroscience , biology , central nervous system , organic chemistry
Fresh myelin, isolated from brainstems of adult rats, was incubated in the presence of Cu 2+ and H 2 O 2 . Electrophoretic analysis of the reisolated myelin membrane revealed a gradual loss of the protein moiety from the characteristic pattern and an increase in aggregated material appearing at the origin of the gel. The aggregation of proteins was time‐dependent and was concomitant with the accumulation of lipid peroxidation products reactive with thiobarbituric acid. Furthermore, during the course of incubation, there was a gradual decrease in the amount of recovered light myelin and a quantitatively similar increase in heavier myelin subfractions. The aggregation of proteins seems not to be directly related to the buoyant densities of myelin fragments. The peroxidative damage to the myelin proteins may be an important contributor to pathochemistry of myelin sheath, in particular, and in general it implies the susceptibility of the protein moiety of cell membranes to oxygen‐induced deterioration.