Abstract
THE repression of β-galactosidase in Escherichia coli has been demonstrated to be sensitive to 2,4-dinitrophenol1. This presumably indicates that high energy phosphate bonds are involved. Alkaline phosphatase is repressed by ortho-phosphate in the medium. We have used this as a test to determine whether high energy phosphate bonds are essential to the mechanism of enzyme repression. Is the intracellular repressing phosphate ortho-phosphate or must it participate in a high energy compound for the formation of “active repressor” ?
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BOWNE, S., ONDREY, J. & WISE, J. Intracellular Repressor of Alkaline Phosphatase. Nature 211, 980 (1966). https://doi.org/10.1038/211980a0
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DOI: https://doi.org/10.1038/211980a0
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