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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Extra resources for Advances in Research and Applications
Biophys. Res. Commun. 45, 1115. , and Dai, V. D. (1967). Eur. J. Biochem. 3, 132. Dombrowski, J. , and Lambooy, J. P. (1973). Arch Biochem. Biophys. 159, 378. BIOCHEMISTRY O F COVALENTLY BOUND FLAVINS 43 Dudley, K. , and Hemmerich, P. (1967). Helv. Chim. Actu 50, 355. Edmondson, D. E. (1974). Biochemistry (in press). Edmondson, D. , and Singer, T. P. (1973). J. Biol. Chem. 248, 8144. Edmondson, D. , and Tollin, G. (1971). Biochemistry 10, 113. Erwin, V. , and Hellerman, L. (1967). J. Biol. Chem.
1973). , 1972). IV. OTHER ENZYMES CONTAINING COVALENTLY LINKEDFLAVINS A. DIMETHYLGLYCINE DEHYDROGENASE It has been suggested (Frisell and Mackenzie, 1962, 1970) that the dimethylglycine dehydrogenase of mammalian liver mitochondria containa covalently bound flavin. The evidence presented is not persuasive, 34 THOMAS P. SINGER AND WILLIAM C. KENNEY however, for the reasons already discussed under sarcosine dehydrogenase (Section 11, D ) , except that this enzyme has been even less extensively purified and that, in this instance, supporting evidence from enzyme induction in bacteria is not available.
After performic acid oxidation. On paper chromat,ograms, Whatman No. 1 paper, descending, n-butanol-acetic acid-H20 (4:2: 2, v/v/v). ,5, 5 b this is readily detected by an increase in fluorescence (Table IV) and a hypsochrornic shift of the optical (Fig. 13) and fluorescence spectra (Fig. 16). , 1967) that the second absorption pcak of the flavin is at 340-350 nm instead FIG. 15. Strurtnre of the flavin peptide from monoamine oxidase. R is rest of FAD in native enzyme or rest, of FMN in pure peptide; R, is serylglgcylglyrine; R, is tyrosyl.
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.)