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By Robert S. Harris, Paul L. Munson, Egon Diczfalusy, John Glover, Kenneth V. Thimann, Ira G. Wool and John A. Loraine (Eds.)

ISBN-10: 0080866298

ISBN-13: 9780080866291

ISBN-10: 0127098321

ISBN-13: 9780127098326

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T See second footnote on page 36. 38 THOMAS P. SINGER AND WILLIAM C. KENNEY vitro experiments, mammalian proteolytic enzymes digest succinate dehydrogenase all the way to 8a-histidyl-FAD, which is readily attacked by nucleotide pyrophosphatase and phosphatases to yield histidyl riboflavin, and it is highly probable that these processes occur in vivo as well. It is desirable, therefore, to delineate clearly the steps in the metabolic breakdown of enzymes containing covalently bound flavin. , 1973).

Biophys. Actn 153, 854. , and Decker, K. Eur. J . Biochem. 29, 152. , and Hemmerich, P. Helv. Chim. Actn 49, 2353. , and Massey, V. J . B i d . Chem. 244, 4007. , Magni, G . , and Nemes-Nanasi, E. , Fed. Eur. Biochem. , 6th, 1869 p. 73. , and Yasunobu, K. T. (1966). Biochem. Biophys. Res. Commun. 23, 324. Neal, R. A. J . Biol. Chem. 245, 2599. Patek, D. ,and Frisell, W. R. Arch. Biochem. Riophys. 150, 347. Patek, D. , Dahl, C. , and Frisell, W. R. (1972). Biochem. Biophys. Res. Commun. 46, 885.

0 after performic acid oxidation and subtraction of the contribution of histidyl flavin from this value. I t should also be remembered that in certain flavin peptides (Chromatiuna cytochrome cS5? peptic peptide and tryptic-chymotryptic peptide of p-cyclopiazonate oxidocyclase) the fluorescence properties are enormously altered because of noncovalent interaction of the flavin with certain amino acyl residues within the pcptide. Perhaps the most serious dilemma is that other types of covalently bound flavin may be detected in the future, estimation of which requires altogether different procedures.

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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.)


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