Albu, Titus V.
Kim, Jisook; Santiago, Manuel F.
University of Tennessee at Chattanooga
Place of Publication
Quinones are the metabolites of a class of chemicals known as polycyclic aromatic hydrocarbons. These chemicals have been found to be toxic in the environment, especially when interacting with certain proteins. In this study, we investigated the modification of Lysozyme and Ribonuclease A by a series of benzoquinones as well as few naphthoquinones. Fluorescence spectroscopy was used to measure the degree of modification of Lysozyme and Ribonuclease A when incubated with quinones at differing concentrations and for various times. All reactions, unless noted, were carried out in a phosphate buffer (pH=7.0) at 37°C to mimic physiological conditions. The fluorescence intensity of modified protein was shown to be less than that of unmodified protein, and effects of quinone substituents were examined. UV-VIS spectroscopy was also utilized to monitor adduct formation and other protein modifications. This study adds to our understanding of the effects of quinones on biological systems.
B. S.; An honors thesis submitted to the faculty of the University of Tennessee at Chattanooga in partial fulfillment of the requirements of the degree of Bachelor of Science.
Quinone; Polycyclic aromatic hydrocarbons -- Toxicology
viii, 100 leaves
Thomas, Charles A. Jr, "Fluorescence and UV-VIS studies of quinone-induced protein modifications" (2017). Honors Theses.