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COPPER AMINE OXIDASES: STUDIES AIMED AT THE IDENTIFICATION OF THE ORGANIC COFACTOR STRUCTURE

Author
SCALZO, THERESA ROSE
Physical Description
247 pages
Additional Creators
Pennsylvania State University
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Summary
The structure of the organic cofactor in copper amine oxidases was investigated. Hamilton earlier proposed that the cofactor could be a modified flavin open at the 5-ring position with a carbonyl or imine substituent at the 4a position, and the working part of the molecule being the pyrimidine ring. Based on the proposed model, attempts to remove the bound cofactor by a condensation reaction with o-phenylenediamine to produce alloxazine under the conditions given in this thesis failed. Characterization was then made by derivatization of the enzyme with substituted phenylhydrazines and hydroxylamine, and comparison of the UV-VIS absorption spectra of the enzyme derivatives with the corresponding derivatives of 5,6-(N-methylphenyl) diaminouracil and pyridoxal. The absorption maxima of the enzyme derivatives were closer to the absorption maxima of the uracil model than the pyridoxal model. The visible absorption spectra of the uracil model p-methoxyphenylhydrazone overlapped the resonances of the corresponding copper-free enzyme derivative, and the spectral shape of the uracil model p-nitrophenylhydrazone at pH 13 was identical to the enzyme derivative's at pH 9. The pyridoxal derivatives did not resemble the enzyme derivative spectra, and it was concluded from this data that pyridoxal could not be the cofactor.
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Dissertation Note
Ph.D. The Pennsylvania State University 1984.
Note
Source: Dissertation Abstracts International, Volume: 46-01, Section: B, page: 1700.
Part Of
Dissertation Abstracts International
46-01B
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