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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.