Open AccessPurification of a Specific tRNA by Sepharose-Bound Enzyme
Author(s) -
Jeffrey L. Denburg,
Marlene DeLuca
Publication year - 1970
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.67.2.1057
Subject(s) - transfer rna , sepharose , enzyme , escherichia coli , biochemistry , amino acyl trna synthetases , affinity chromatography , covalent bond , chemistry , biology , rna , organic chemistry , gene
A new procedure for measuring binding of tRNA to aminoacyl-tRNA synthetases is described. The purified isoleucyl-tRNA synthetase fromEscherichia 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.