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DC Field | Value | Language |
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dc.contributor.advisor | McCalla, D.R. | - |
dc.contributor.author | Anderson, Gregory | - |
dc.date.accessioned | 2019-06-18T13:59:43Z | - |
dc.date.available | 2019-06-18T13:59:43Z | - |
dc.date.issued | 1983-09 | - |
dc.identifier.uri | http://hdl.handle.net/11375/24553 | - |
dc.description.abstract | In recent years the nitrated polycyclic aromatic hydrocarbons (nitroPAH's) have been recognized as powerful mutagens in the Ames Salmonella test. Most nitroPAH’s are direct-acting mutagens in the Ames test i.e. they induce mutation in the absence of S9, and appear to be activated through nitroreduction by bacterial enzymes. Others, however, such as 3-nitroperylene, are indirect-acting mutagens and show maximum activity only when S9 is present. Studies using the Ames test have indicated that the cytochrome P-450-dependent mixed function oxidase system of S9 is responsible for the activation of 3-nitroperylene to mutagenic species. However, the pattern of P-450 isozymes involved in this process appears to be different from that involved in the conversion of most PAH's, such as the standard indirect-acting mutagen benzo(a)pyrene (B(a)P), to proximate mutagens. 6-NitroB(a)P, in contrast, behaves in an analogous manner to its parent hydrocarbon. Using appropriate Salmonella mutants, the activation of 3-nitroperylene was found to require bacterial involvement, although the nature of the bacterial contribution has yet to be determined. Studies with other mutants have indicated that nitroreduction, at least as a primary activation step, does not appear to be important. Incubation of 3-nitroperylene with high concentrations of S9 led to the formation of a number of metabolites, of which phenolic derivatives were prominent. In addition, S9-derived microsomes were able to catalyse the conversion of 3-nitroperylene to species which were able to bind to protein and DNA. Under the conditions employed in these binding studies, 3-nitroperylene appears to be acting like a simple PAH, and such experiments with very high concentrations of liver protein may be unrepresentative of the processes responsible for the mutagenesis of the compound. | en_US |
dc.language.iso | en | en_US |
dc.subject | 3-nitroperylene | en_US |
dc.subject | nitrated polycyclic aromatic hydrocarbon | en_US |
dc.subject | polycyclic aromatic hydrocarbon | en_US |
dc.subject | aromatic hydrocarbon | en_US |
dc.subject | mutagenicity | en_US |
dc.subject | metabolism | en_US |
dc.subject | macromolecule binding | en_US |
dc.subject | biochemistry | en_US |
dc.subject | mutagenicity, metabolism and macromolecule binding of 3-nitroperylene | en_US |
dc.subject | mutagenicity and metabolism of 3-nitroperylene | en_US |
dc.title | The Mutagenicity, metabolism and macromolecule binding of the nitrated polycyclic aromatic hydrocarbon 3-nitroperylene | en_US |
dc.title.alternative | The Mutagenicity and metabolism of 3-nitroperylene | en_US |
dc.type | Thesis | en_US |
dc.contributor.department | Biochemistry | en_US |
dc.description.degreetype | Thesis | en_US |
dc.description.degree | Master of Science (MSc) | en_US |
Appears in Collections: | Digitized Open Access Dissertations and Theses |
Files in This Item:
File | Description | Size | Format | |
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Anderson_Gregory_J_1983Sep_masters.pdf | 5.64 MB | Adobe PDF | View/Open |
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