title: Purification of a specific tRNA by Sepharose-bound enzyme.
abstract: A new procedure for measuring binding of tRNA to aminoacyl-tRNA synthetases is described. The purified isoleucyl-tRNA synthetase from Escherichia coli can be covalently bound to activated Sepharose with retention of approximately 40% of the original enzymatic activity. If crude tRNA is passed through a small column of enzyme-Sepharose, isoleucyl-tRNA is preferentially retained. The procedure can be used as a means of purifying specific tRNA molecules.
mesh_terms: D002247:Carbon Isotopes; D002845:Chromatography; D004926:Escherichia coli / Q000201:enzymology; D007532:Isoleucine; D008025:Ligases; D008722:Methods; D010759:Phosphorus Isotopes; D011134:Polysaccharides; D011485:Protein Binding; D012343:RNA, Transfer / Q000302:isolation & purification*
chemical_list: D002247:Carbon Isotopes; D010759:Phosphorus Isotopes; D011134:Polysaccharides; D007532:Isoleucine; D012343:RNA, Transfer; D008025:Ligases