Evidence of the carboxymethylation of nascent peptide chains on ribosomes |
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Authors: | Jan-Kan Chen Maurice Liss |
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Affiliation: | Department of Biology, Boston College Chestnut Hill, Mass. 02167 USA |
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Abstract: | Protein carboxymethylase from bovine anterior pituitary is found to be capable of carboxymethylating proteins in an in vitro protein synthesizing system which includes S-adenosyl-L-methionine-[14C methyl], wheat germ ribosomes and oviduct mRNA. Optimal carboxymethylation is inhibited by puromycin indicating the requirement for de novo protein synthesis. Ultracentrifugal profiles show that carboxymethylated proteins are associated with ribosomal absorption peaks. This is consistent with the carboxymethylation of proteins occurring on nascent peptide chains. |
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