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- W1567475756 abstract "We purified the dsdC gene product, the specific activator of dsdA (D-serine deaminase) gene expression, to about 25% homogeneity from a strain in which its expression was amplified 100-fold. The purification involved, successively: DNase and high-salt treatment of cell extracts, DNA-cellulose chromatography, and Dyematrex (Amicon Corp.) column chromatography. We identified the protein as a discrete spot on two-dimensional O'Farrell gels after the DNA-cellulose step and quantitated it by densitometry. The active form was found to be a dimer. We estimated that there were eight activator dimers per wild-type cell. The activator is a slightly basic protein, with an experimental Km for its ligand D-serine of about 7 X 10(-6)M. The low concentration of the activator in wild-type cells and its autorepression may explain the previously observed partial dominance of dsdC+ in dsdCc/dsdC+ merodiploids." @default.
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- W1567475756 date "1984-10-01" @default.
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- W1567475756 title "Purification and characterization of D-serine deaminase activator protein" @default.
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- W1567475756 doi "https://doi.org/10.1128/jb.160.1.42-49.1984" @default.
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