Salvage of pyrimidine nucleosides and bases by S. griseus and the regulation of aspartate transcarbamoylase (ATCase) were studied. The velocity-substrate curve for S. griseus ATCase was hyperbolic for both aspartate and carbamoylphosphate. The enzyme activity was diminished in the presence of ATP, CTP, or UTP. The synthesis of ATCase was repressed in cells grown in the presence of exogenous uracil. The specific activity of cells grown with uracil was 43 percent of that for cells grown in minimal medium only. Maximal ATCase and dihydroorotase activities were found in the same column fraction after size-exclusion chromatography, suggesting that both activities could reside in the same polypeptide. The pyrimidine salvage enzymes cytosine deaminase and uridine phosphorylase were identified in S. griseus using HPLC reversed-phase chromatography.
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc278710 |
| Date | 08 1900 |
| Creators | Hughes, Lee E. (Lee Everette) |
| Contributors | O'Donovan, Gerard A., Benjamin, Robert C., Shanley, Mark Stephen |
| Publisher | University of North Texas |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | Text |
| Rights | Public, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved., Hughes, Lee E. (Lee Everette) |
Page generated in 0.0023 seconds