The binding of aminoacyl-tRNA synthetases to triazine dye conjugates

The binding of thirteen aminoacyl-tRNA synthetases to thirty two immobilised procion dyes has been investigated. Most dyes bind one or more enzymes. The amino acid substrates are not normally potent eluants, with the notable exception of tryptophan eluting tryptophanyl-tRNA synthetase from Brown MX-...

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Veröffentlicht in:Nucleic acids research 1979-11, Vol.7 (6), p.1579-1591
Hauptverfasser: Bruton, Chris J., Atkinson, Tony
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Atkinson, Tony
description The binding of thirteen aminoacyl-tRNA synthetases to thirty two immobilised procion dyes has been investigated. Most dyes bind one or more enzymes. The amino acid substrates are not normally potent eluants, with the notable exception of tryptophan eluting tryptophanyl-tRNA synthetase from Brown MX-5BR. Phosphate is frequently extremely effective, much more than expected by simple considerations of ionic strength, indicating that many of the dyes are able to mimic the phosphate groups of the phosphodiester backbone of the nucleic acid. Procedures for the purification of methionyl-, tryptophanyl- and tyrosyl-tRNA synthetases are presented and compared to the conventional purifications of these enzymes. The results indicate the general applicability of these dye columns to the purification of most enzymes of nucleic acid metabolism and the necessity of investigating as many different dyes as possible for any individual enzyme.
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subjects Amino Acyl-tRNA Synthetases - isolation & purification
Amino Acyl-tRNA Synthetases - metabolism
Binding Sites
Coloring Agents - pharmacology
Geobacillus stearothermophilus
Protein Binding
Structure-Activity Relationship
Triazines - pharmacology
title The binding of aminoacyl-tRNA synthetases to triazine dye conjugates
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