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-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 of nucleic acid metabolism and the necessity of investigating as many different dyes as possible for any individual enzyme.
D000604:Amino Acyl-tRNA Synthetases / Q000302:isolation & purification / Q000378:metabolism*; D001665:Binding Sites; D004396:Coloring Agents / Q000494:pharmacology; D001411:Geobacillus stearothermophilus; D011485:Protein Binding; D013329:Structure-Activity Relationship; D014227:Triazines / Q000494:pharmacology
D004396:Coloring Agents; D014227:Triazines; D000604:Amino Acyl-tRNA Synthetases