This investigation describes the isolation and purification of a deacetylase from trout testes (Salmo gairdnerii) and its initial characterization, the results of which are summarized as follows;
- Histone deacetylase activity was demonstrated in the 230,000 x g supernatant fraction of trout testes by a new and sensitive assay.
- The deacetylase was purified by salt precipitation, molecular seive chromatography and subsequent ion exchange chromatography.
- Two major fractions of enzyme activity were demonstratable with their approximate molecular sizes estimated.
- The specificity of the enzyme towards different histone fractions appeared to undergo dramatic changes, depending on prior treatments.
- Preliminary results as these furnished some basis for speculation regarding (a) the possible significance of deacetylation not only as a histone modification process but also in the role of gene regulation and (b) the logical prediction as to the existence of enzyme species exhibiting varying substrate specificities to cope with the distinct classes of histones unmasked in trout testes. / Medicine, Faculty of / Biochemistry and Molecular Biology, Department of / Graduate
| Identifer | oai:union.ndltd.org:UBC/oai:circle.library.ubc.ca:2429/32566 |
| Date | January 1972 |
| Creators | Stevenson, Barry W. A. |
| 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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