Evidence of the carboxymethylation of nascent peptide chains on ribosomes

Jan Kan Chen; Maurice Liss

doi:10.1016/0006-291X(78)90291-7

Evidence of the carboxymethylation of nascent peptide chains on ribosomes

Jan Kan Chen^*, Maurice Liss

^*Corresponding author for this work

Boston College

Research output: Contribution to journal › Journal Article › peer-review

14 Scopus citations

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.

Original language	English
Pages (from-to)	261-268
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	84
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(78)90291-7
State	Published - 14 09 1978
Externally published	Yes

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title = "Evidence of the carboxymethylation of nascent peptide chains on ribosomes",

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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AU - Liss, Maurice

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N2 - 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.

AB - 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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JO - Biochemical and Biophysical Research Communications

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Evidence of the carboxymethylation of nascent peptide chains on ribosomes

Abstract

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