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- W2021757419 abstract "A glutamyl-tRNA synthetase has been purified to homogeneity from Rhizobium meliloti, using reversed-phase chromatography as the last step. Amino acid sequencing of the amino-terminal region of the enzyme indicates that it contains a single polypeptide, whose molecular weight is about 54 000, as judged by SDS–gel electrophoresis. The primary structures of the amino-terminus region and of an internal peptide obtained by cleavage of the enzyme with CNBr have similarities of 58 and 48% with regions of the glutamyl-tRNA sythetase of Escherichia coli; these are thought to be involved in the binding of ATP and tRNA, respectively. The small amount of glutamyl-tRNA synthetase present in R. meliloti is consistent with the metabolic regulation of the biosynthesis of many aminoacyl-tRNA synthetases.Key words: glutamyl-tRNA synthetase, Rhizobium meliloti, purification, reverse-phase chromatography, amino acid sequence." @default.
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- W2021757419 date "1989-10-01" @default.
- W2021757419 modified "2023-09-27" @default.
- W2021757419 title "Purification and partial amino acid sequence of a glutamyl-tRNA synthetase from Rhizobium meliloti" @default.
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- W2021757419 doi "https://doi.org/10.1139/o89-101" @default.
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