By Robert S. Harris, Paul L. Munson, Egon Diczfalusy, John Glover, Kenneth V. Thimann, Ira G. Wool and John A. Loraine (Eds.)
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1972a). 2. Natiirforsch. B 27, 1073. , and Decker K. (1972b). Eur. J. Biochem. 29, 143. , and Giordano, M. G. (1963). Arch. Biochem. Biophys. 101, 423. , Giordano, M. , and Giovenco, M. A. (1964). Biochem. Biophys. Res. Commun. 14, 408. Chelkowski, J. (1971). Bull. Acad. Pol. , Ser. Sci. Biol. 19, 153. Chi, T. , Wang, Y. , Tsou, C. , Fang, Y. , and Yu, C. H. (1965). Sci. Sinica 14, 1193. Clark, W. M. (1960). ” Williams & Wilkins, Baltimore, Maryland. Coles, C. , Tisdale, H. , Kenney, W. , and Singer, T.
1968). The flavin obtained by the urea procedure had a modified absorption spectrum relative to riboflavin and was nonfluorescent. While release of a flavin peptidc from covalent linkage to the protein by proteolytic digestion in water-soluble form is to be expected from prior results with succinate dehydrogeiiase and moiioamine oxidase, release by the other agents listed, particularly urea, is quite unexpected. The fact that prolonged treatment with 8 M urea indeed dissociates the flavin from the rest of thc protein has been confirmed by Hendriks and Cronin (1971), but it has been considered" that the agent responsiblc is the cyanate impurity present in urea preparations, rather than urea itself.
Hyperconjugation and tautomerization will shift a proton from the 8a-methylene to N-1, resulting in the 8a-position being more susceptible to nucleophilic attack by, for example, an imidazole nitrogen of a histidyl residue or a thiol group of a cysteinyl residue. The resultiiig adduct would be the reduced form of covalently bound FAD, which is then readily oxidized. As yet there is no evidence to decide whether or not the attachment of flavin to the apoenzyme is a n enzymatic process. , and Kearney, E.
Advances in Research and Applications by Robert S. Harris, Paul L. Munson, Egon Diczfalusy, John Glover, Kenneth V. Thimann, Ira G. Wool and John A. Loraine (Eds.)