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- W2083825575 abstract "Abstract The flavin prosthetic group of sarcosine dehydrogenase from rat liver mitochondria has been separated from other mitochondrial acid-extractable and acid-non-extractable flavins and purified by chromatography on Florisil, Dowex 1, CM Sephadex, and DEAE-Sephadex. The flavin is similar to that isolated previously from succinate dehydrogenase of beef and pig heart mitochondria. Characteristically, the flavin cannot be released from the apoenzyme by precipitation of the protein with trichloracetic acid, but can be solubilized by hydrolysis of the protein with trypsin, α-chymotrypsin, and other proteases. The oxidized mononucleotide form of the flavin exhibits an absorption spectrum almost identical with that of the flavin of succinate dehydrogenase. Maxima occur at 351 and 445 mμ with a 351:445 mμ ratio of 0.77. A maximum is found at 268 mμ with a 268:445 mμ ratio of 2.9. The fluorescence emission of the flavin occurs at approximately 523 mμ and exhibits a maximum fluorescence at pH 3, even when isolated as a mononucleotide. The data support the conclusion that the native state of the flavin is a dinucleotide. The midpoint reduction potential at pH 7.0 of the flavin is approximately −167 mV at 26 °C." @default.
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- W2083825575 date "1972-06-01" @default.
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- W2083825575 title "Purification and characterization of the flavin prosthetic group of sarcosine dehydrogenase" @default.
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- W2083825575 doi "https://doi.org/10.1016/0003-9861(72)90048-3" @default.
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