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The purification and properties of ribonucleases Roy, Kenneth Leo Joseph

Abstract

The purification of ribonucleases T₁ and T₂ from Ta-kadiastase has been carried out to provide enzymes of high purity and known specificity for structural studies on s-RNA. These purifications involved acid treatment, acetone fractionation, gel filtration on Sephadex and ion-exchange chromatography on substituted celluloses. Satisfactorily pure RNase T₁ has been obtained and its specificity has been confirmed. Further purification of RNase T₂ might be desireable but some studies using chemically synthesized substrates have been carried out on the most highly purified fraction yet obtained. Partial purification of an RNase present in a different diastase preparation involved heat, acid, acetone fractionation and anion exchange chromatography. Information is not yet available on its specificity because of the small quantities isolated.

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