Mouse brain protein composition during postnatal development: an electrophoretic analysis.

Changes in the concentrations of mouse brain proteins during postnatal maturation were characterized by a combination of subcellular fractionation and electrophoresis. Sodium dodecyl sulfate gel electrophoresis revealed changing protein concentrations in fractions enriched in nuclei, mitochondria plus synaptic endings, microsomes and cytosol. Postnatal maturational changes in protein concentrations were most pronounced in fractions of purified myelin membranes. The use of exponential gradient gels resulted in increased resolution of low molecular weight myelin proteins. Nuclei treated with Triton X-100 exhibited no change in relative histone concentrations during brain maturation. Nonnuclear contamination of untreated nuclear fractions was shown to be a potential source of erroneous interpretations. These findings are discussed in terms of genetic products and sodium dodecyl sulfate polyacrylamide gel electrophoresis resolution.