1971•Journal of Biological ChemistryOpen access

Purification of an Escherichia coli Leucine Suppressor Transfer Ribonucleic Acid and Its Aminoacylation by the Homologous Leucyl-Transfer Ribonucleic Acid Synthetase

Hiroshi Hayashi, Dieter G. Söll

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Abstract

Abstract The leucine amber suppressor tRNA of an Escherichia coli strain carrying the Su6+ gene has been purified completely by benzoylated DEAE-cellulose chromatography. This tRNA mediates in vitro polyleucine formation with poly r(U-A-G). In the aminoacylation reaction with the pure Escherichia coli leucyl-tRNA synthetase it possesses the same Km (5 x 10-8 m) as the other tRNAleu species.

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Abstract The leucine amber suppressor tRNA of an Escherichia coli strain carrying the Su6+ gene has been purified completely by benzoylated DEAE-cellulose chromatography. This tRNA mediates in vitro polyleucine formation with poly r(U-A-G). In the aminoacylation reaction with the pure Escherichia coli leucyl-tRNA synthetase it possesses the same Km (5 x 10-8 m) as the other tRNAleu species.

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Available abstract

Abstract The leucine amber suppressor tRNA of an Escherichia coli strain carrying the Su6+ gene has been purified completely by benzoylated DEAE-cellulose chromatography. This tRNA mediates in vitro polyleucine formation with poly r(U-A-G). In the aminoacylation reaction with the pure Escherichia coli leucyl-tRNA synthetase it possesses the same Km (5 x 10-8 m) as the other tRNAleu species.

Key concepts: Aminoacylation, Transfer RNA, Escherichia coli, Leucine, Homologous chromosome, Biochemistry, Chemistry, Amino Acyl-tRNA Synthetases

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