Denburg J, DeLuca M
Proc Natl Acad Sci U S A. 1970 Oct;67(2):1057-62. doi: 10.1073/pnas.67.2.1057.
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.