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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8. p H dependence of fluorescence of tr3ptic-cligmotryptic flavin peptide of thiamine dehydrogenase at the FMN level. , contains no metals, the absorption spectrum is characteristic of flavoproteins, with maxima a t 368 and 444 nm, shoulders at 424 and 470 nm, and a minimum a t 404 nm. The flavin prosthetic group was shown to be resistant to dissociation from the protein on heating, precipitation with trichloroacetic acid, or incubation with 6 M guanidine. , 1974a). It was shown that tryptic-chymotryptic digestion releases the flavin in acid-soluble form.
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.)