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. 1970 Oct;67(2):1057–1062. doi: 10.1073/pnas.67.2.1057

Purification of a Specific tRNA by Sepharose-Bound Enzyme*

Jeffrey Denburg 1,2, Marlene DeLuca 1,2,†
PMCID: PMC283312  PMID: 4943171

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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