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Updated: Jul 30, 2026

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
Published on: January 11, 2017
[Modification of the histidine in rat skeletal muscle deaminase by diethylpyrocarbonate]
Abstract:
Diethylpyrocarbonate inactivated rat skeletal muscle AMP deaminase in 10 mM phosphate buffer, pH 6.5, at 23 degrees with the second order rate constant of 580 M-1.min-1. Absorbtion at 240 nm was concomitantly increase. Enzyme activity can be restored by hydroxylamine. The pH-dependence of inactivation indicates the involvement of a group with pKa 6.9. The data suggest that modification of one histidyl residue per subunit inactivates the activity of tetrameric AMP deaminase.
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