Abstract
WE have obtained from pig liver a flavoprotein in highly purified form which catalyses specifically the oxidation of aldehydes to their corresponding acids. The prosthetic group of this enzyme is flavinadenine dinucleotide. In the presence of acetaldehyde the enzyme is rapidly reduced to its leuco form, and the leuco form is autoxidizable in air. The mechanism of the catalysis, therefore, involves a cycle of reduction of the flavoprotein by the substrate followed by oxidation of the leuco form by molecular oxygen or any other suitable hydrogen acceptor. One molecule of the enzyme catalyses the oxidation of about 550 molecules of acetaldehyde per minute at 38°. Our best preparations of the enzyme transfer 2700 μl.H2 per mgm. protein per hour (Qmethylene blue 2700). The flavinphosphate content of the preparation as determined by direct estimation is 0·17 per cent. There appears to be some coloured grouping other than flavin which is associated with the enzyme molecule.
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SUBRAHMANYAN, V., GREEN, D. & GORDON, A. Isolation of a Catalytically Active Flavoprotein from Liver. Nature 144, 1016 (1939). https://doi.org/10.1038/1441016a0
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DOI: https://doi.org/10.1038/1441016a0
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