Résultats de la recherche

Yeast phenylalanyl--tRNA synthetase. Stimulation of the hydrolysis of enzyme bound aminoacyladenylate upon binding of tRNA

Yeast phenylalanyl-tRNA synthetase: evidence for the triggering of an AMP--ATP exchange by tRNA.

Fluorimetric study of the complex between yeast phenylalanyl-tRNA synthetase and tRNA-Phe. 1. Changes in the conformation of the enzyme and tRNA; modification of the Wybutine neighbourhood.

Fluorimetric study of the complex between yeast phenylalanyl-tRNA synthetase and tRNA-Phe. 2. Evidence for an asymmetric behaviour of the enzyme.

Fast kinetic study of yeast phenylalanyl-tRNA synthetase: role of tRNAPhe in the discrimination between tyrosine and phenylalanine

Yeast phenylalanyl-tRNA synthetase. Affinity and photoaffinity labelling of the stereospecific binding sites.

Fast kinetic study of yeast phenylalanyl-tRNA synthetase: an efficient discrimination between tyrosine and phenylalanine at the level of the aminoacyladenylate-enzyme complex.

Purification of yeast phenylalanyl-tRNA synthetase by affinity chromatography, on a tRNA(Phe)-sepharose column.

Phenylalanyl-tRNA synthetase of baker&#039;s yeast. Modulation of adenosine triphosphate-pyrophosphate exchange by transfer ribonucleic acid.

Yeast phenylalanyl-tRNA synthetase: symmetric behavior of the enzyme during activation of phenylalanine as shown by a rapid kinetic investigation.

Crosslinking of N-acetyl-phenylalanyl [s4U]tRNAPhe to protein S10 in the ribosomal P site.

[Analogs of nucleoside polyphosphates. 3. Action of adenosine 5&#039;-phosphohypophosphate on hexokinase and on valyl-tRNA synthetase].

Study of the interaction between yeast tRNAphe and yeast phenylalanyl-tRNA synthetase by monochromatic ultraviolet irradiation at various wavelengths. Advantages and limits of the method.

Lack of correlation between affinity of the tRNA for the aminoacyl-tRNA synthetase and aminoacylation capacity as studied with modified tRNAPhe.

Covalent modification of phenylalanyl-tRNA synthetase with phenylalanine during the amino acid activation reaction catalyzed by the enzyme.

Mutual adaptation of yeast tRNAPhe and phenylalanyl-tRNA synthetase: Possible role of tryptophan residues and long range interactions.

Quantitative study of the ionic interactions between yeast tRNAVal and tRNAPhe and their cognate aminoacyl-tRNA ligases

Yeast phenylalanyl-tRNA synthetase: properties of the sulfhydryl groups; evidence for -SH requirement in tRNA acylation.

Yeast phenylalanyl-tRNA synthetase: isolation of subunits on organomercurial-sepharose columns.

Conformational activation of aminoacyl-tRNA synthetases upon binding of tRNA. A facet of a multi-step adaptation process leading to the optimal biological activity.