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. 1967 Oct;105(1):17–24. doi: 10.1042/bj1050017

Purification and properties of methionyl-transfer-ribonucleic acid synthetase from Escherichia coli

R L Heinrikson 1,*, B S Hartley 1
PMCID: PMC1198268  PMID: 4293517

Abstract

1. Methionyl-t-RNA synthetase (where t-RNA denotes `soluble' or transfer RNA) has been purified to apparent homogeneity from a ribonuclease I-free strain of Escherichia coli. Polyacrylamide-gel electrophoresis of the final product revealed a single band. The purified enzyme catalyses the exchange of 450μmoles of pyrophosphate into ATP/mg. in 15min. at 37°. 2. Methionyl-t-RNA synthetase is specific for the l-isomer of methionine, but appears to catalyse the methionylation of two distinct species of t-RNA, both of which are specific for methionine, but only one of which may be subsequently formylated. 3. The Michaelis constant for l-methionine is 2×10−4m in the ATP–PPi exchange assay and 2×10−5m for the acylation of t-RNA. 4. Gel filtration of both crude and highly purified preparations of methionyl-t-RNA synthetase on Sephadex G-200 indicates that the active species of enzyme has a molecular weight of about 190000. The amino acid composition of the enzyme is similar to those reported for the isoleucine and tyrosine enzymes from E. coli.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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