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- W2069006172 abstract "A multimeric alcohol oxidase from Aspergillus terreus was dissociated and simultaneously deflavinated into catalytically inactive FAD-free subunits when incubated with 0.74 M beta-mercaptoethanol (beta-ME) for 8 h at 4 degrees C. This dissociation process had traversed through two FAD-associated intermediate proteins, between these one of them showed the enzyme activity. On removal of beta-ME, the multimeric apoprotein was regenerated, which was, however, catalytically inactive. Reactivation of the FAD supplemented apoprotein was accomplished only after incubating with the substrate. This catalytic reactivation was a slow process as evident from the prolonged FAD emission quenching. The dissociation and re-association phenomena were demonstrated by using dynamic light scattering, size exclusion chromatographic, confocal laser scan microscopic and native PAGE analyses. The solvent effect caused by the high concentration of beta-ME is attributed to the observed dissociation and linked deflavination of these multimeric alcohol oxidase protein particles." @default.
- W2069006172 created "2016-06-24" @default.
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- W2069006172 date "2008-12-06" @default.
- W2069006172 modified "2023-09-25" @default.
- W2069006172 title "Dissociation and Reconstitution Studies of a Broad Substrate Specific Multimeric Alcohol Oxidase Protein Produced by Aspergillus terreus" @default.
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- W2069006172 doi "https://doi.org/10.1093/jb/mvn163" @default.
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