Abstract
Abstract—The incorporation of [14C]lysine into various brain proteins was studied. The proteins of different areas of the auditory system and cortical subcellular fractions were analysed using a disc electrophoretic technique that allows both protein and radioactivity assays along the gels. The highest level of incorporation was found in the mid brain nuclei, particularly the inferior colliculus, and was lowest in the auditory cortex proteins. This was true for both saline soluble proteins and proteins solubilized by Triton X‐100 treatment. Of the subcellular fractions, the highest level of activity was found in the microsomal fraction. Considerable radioactivity was also found in the proteins isolated from the synaptosome‐rich fraction. Of particular interest in this fraction was a slow migrating protein band which was soluble in Triton X‐100, had a high specific activity, and appeared to be synaptosome specific. These observations are in concurrence with the hypothesis that the nerve ending contains protein synthesizing machinery.
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