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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Therefore, a procedure for the large-scale preparation of outer membranes was elaborated and monoamirie oxidase extracted from this source material was virtually free from succinate dehydrogenase. This permitted the unambiguous demonstration of the properties of the covalently bound flavin of mitochondria1 monoamine oxidase and identification of its chemical nature, as described below. 1. , 1971a,b) were BIOCHEMISTRY O F COVALENTLY BOUND FLAVINS 21 FIG 12. Electron spin resonance spertra of cation radicals of flavins and flavin peptides.

I. (1971). Unpublished results. BIOCHEMISTRS O F COVALENTLY BOUND FLAVINS 27 determiiiation of cysteinyl flavin thioether is both conceptually and practically more difficult and, consequently, no detailed procedure has been published. 0 but increases from about 10% to about 80% of that of riboflavin on oxidation with performic acid. While both of the properties set apart cysteinyl flavin thioethers from histidyl flavin, the latter requires that a t the time of analysis all the cysteinyl flavin be in the reduced (thioether) state.

1974) FEBS Lett. 42, 1. Singer, T. P. and Kearney, E. B. (1960). In “Vitamin Metabolism” (W. Umbreit and M. ), pp. 209-229. Pergamon, Oxford. Singer, T. , Kearney, E. , and Massey, V. (1955). Arch. Biochem. Biophys. 60, 255. Singer, T. , Kearney, E. , and Massey, V. (1956). In “Enzymes: Units of Biological Structure and Function” (0. H. ), pp. 417-432. Academic Press, New York. Singer, T. , and Kearney, E. B. (1957). Arch. Biochem. Biophys. 69, 405. Singer, T. , and Kearney, E. B. (1962). Biochem.

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