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- W1551667110 abstract "Abstract Rabbit muscle 5'-AMP aminohydrolase was shown to be susceptible to a protein concentration-dependent, dilution-induced inactivation at protein concentrations used in normal spectrophotometric assays; i.e. 0.5 µg per ml. Inactivation was less evident at saturating concentrations of substrate and at pH 6.3. These properties accounted for the AMP concentration versus initial velocity profiles which at pH 7.0 and 0.5 µg of enzyme per ml were sigmoidal but hyperbolic at 50 µg per ml; at pH 6.3 substrate saturation versus initial velocity profiles were hyperbolic at both protein concentrations. Kinetic parameters for deamination of AMP determined by stopped flow spectrophotometry at 50 µg per ml where dilution inactivation was not observed are reported as a function of pH. The potassium-activated enzyme exhibits normal Michaelis-Menten kinetics in the pH range 6.15 to 7.2; Vmax = 1730 ± 260 µmoles min-1 mg-1 at 30° and is invariant over the same pH range; Km increases slightly at the higher pH." @default.
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- W1551667110 date "1971-12-01" @default.
- W1551667110 modified "2023-09-30" @default.
- W1551667110 title "5′-Adenosine Monophosphate Aminohydrolase" @default.
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- W1551667110 doi "https://doi.org/10.1016/s0021-9258(19)45878-x" @default.
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