Aldehyde oxidase has been partially purified from Oregon-R-C and tuh(ASU) strains of Drosophila melanogaster using an affinity technique. The two enzymes were subjected to a partial kinetic analysis and found to be very similar to one another. This indicated the problem of elevated aldehyde oxidase activity in tuh(ASU) at key developmental stages (Kuhn and Cunningham, 1976) is due to an abnormal regulation. A comparative isozyme study through the developmental stages showed no major differences between the enzymes indirectly supporting the idea of an abnormal regulation. A comparison of tuh(ASU) with four wild-type strains indicated it may be a fourth allozyme of aldehyde oxidase.
| Identifer | oai:union.ndltd.org:ucf.edu/oai:stars.library.ucf.edu:rtd-1371 |
| Date | 01 January 1977 |
| Creators | Respess, Richard A. |
| Publisher | Florida Technological University |
| Source Sets | University of Central Florida |
| Language | English |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Retrospective Theses and Dissertations |
| Rights | Public Domain |
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