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. / Medicine, Faculty of / Biochemistry and Molecular Biology, Department of / Graduate
| Identifer | oai:union.ndltd.org:UBC/oai:circle.library.ubc.ca:2429/39764 |
| Date | January 1964 |
| Creators | Roy, Kenneth Leo Joseph |
| Publisher | University of British Columbia |
| Source Sets | University of British Columbia |
| Language | English |
| Detected Language | English |
| Type | Text, Thesis/Dissertation |
| Rights | For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use. |
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