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- W2012077400 abstract "1.|The effects of monovalent cations on the kinetic properties and molecular weight of rabbit muscle AMP deaminase (AMP aminohydrolase, EC 3.5.4.6) have been determined and the subunit structure of the enzyme has been examined. 2.|The enzyme is activated by monovalent cations at non-saturating AMP concentrations. K+ is the most effective, followed by Na+, Li+, NH4+ and Rb+ in that order. No stimulation was observed with Cs+ up to 0.5 M. The response to these cations is non-hyperbolic, and both the half-saturating concentrations and the maximal stimulation are different for different cations. 3.|On the removal of activating cations, and at protein concentrations of less than 1 mg/ml the enzyme reversibly dissociates, giving a peak of activity in sucrose density gradient centrifugation corresponding to a molecular weight of approximately 80 000. 4.|Sedimentation to equilibrium in an analytical ultracentrifuge in the absence of activating ions showed a marked increase in the apparent molecular weight with increasing protein concentration. The apparent molecular weight varied from < 100 000 to > 250 000 in the range 1.6–10 mg protein/ml. 5.|After reduction and alkylation, AMP deaminase migrated in sodium dodecyl sulphate-polyacrylamide gels as a single component with molecular weight of 79 000 ± 2000." @default.
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- W2012077400 date "1972-02-01" @default.
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- W2012077400 title "AMP deaminase from rabbit skeletal muscle: The effect of monovalent cations on catalytic activity and molecular weight" @default.
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- W2012077400 doi "https://doi.org/10.1016/0005-2744(72)90253-7" @default.
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