Human tryptophan transfer ribonucleic acid synthetase. Composition, function of thiol groups, and structure of thiol peptides.

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Human tryptophan transfer ribonucleic acid synthetase. Composition, function of thiol groups, and structure of thiol peptides.

Human tryptophanyl-tRNA synthetase resembles its counterpart in Escherichia coli in quaternary structure (alpha2), but differs in molecular weight, amino acid composition, the number of thiol groups, and the relationship of the thiol groups to enzyme activity. Nevertheless, one of the thiol groups resides in a heptapeptide sequence homologous to a heptapeptide sequence containing a thiol group ...

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Tryptophanyl transfer ribonucleic acid synthetase of Escherichia coli. Character of required thiol group and structure of thiol peptides.

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Structure and function of transfer ribonucleic acid. 3. Some properties of a complex between valyl transfer ribonucleic acid synthetase and transfer ribonucleic acid specific for valine.

The formation and some properties of a stable complex between valyl transfer ribonucleic acid synthetase and transfer RNA from yeast have been investigated by three different methods for the isolation of the complex: titration over Sephadex, sucrose gradient centrifugation, and electrophoresis on Pevikon as supporting medium. Transfer RNA specific for valine (tRNAvsl) can be separated into two ...

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The formation of a stable complex between valyl transfer ribonucleic acid synthetase from yeast and transfer RNA specific for valine (tRNAVa’) from the same source has been used as a model for the recognition between enzyme and tRNA. With the use of sucrose gradient centrifugation to isolate the complex, the major fraction of tRNAVal (tRNAp’) was found to retain its ability to form a stable com...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1976

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(17)33432-4