Abstract
Ribosomal protein synthesis was measured with ribosomes isolated from 1-day old and adult mouse brain tissue. When 3H-phe-tRNA was used as the phenylalanine donor, a two fold difference in ribosomal activity was observed. Either mouse brain or E. coli tRNA could participate in brain ribosomal polypeptide synthesis and the maturation-dependent difference in ribosomal activity measured. The difference in the rate of protein synthesis was shown to be associated with the ribosome particles themselves. The incorporation of phenylalanine was shown to be the result of active translocation and was inhibited by diphtheria toxin, N-ethylmaleimide and fusidic acid. Thiostrepton, a potent inhibitor of bacterial peptidyl translocase, did not inhibit brain protein synthesis.
Published Version
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