Steady-state kinetics of aldehyde oxidation by pig liver cytosolic aldehyde dehydrogenase

1988 ◽  
Vol 16 (5) ◽  
pp. 857-858 ◽  
Author(s):  
JEREMY P. HILL ◽  
F. MARK DICKINSON
Keyword(s):  
Steady State ◽  
Aldehyde Dehydrogenase ◽  
Pig Liver ◽  
Steady State Kinetics ◽  
Aldehyde Oxidation ◽  
Kinetics Of

scholarly journals Steady-state kinetic analysis of aldehyde dehydrogenase from human erythrocytes

1992 ◽  
Vol 287 (1) ◽  
pp. 145-150 ◽  
Author(s):  
G T M Henehan ◽  
K F Tipton
Keyword(s):  
Steady State ◽  
Aldehyde Dehydrogenase ◽  
Initial Rate ◽  
Substrate Inhibition ◽  
Human Erythrocytes ◽  
Steady State Kinetics ◽  
Steady State Kinetic ◽  
Sequential Mechanism ◽  
Kinetics Of

The steady-state kinetics of purified cytoplasmic aldehyde dehydrogenase (EC 1.2.1.3) from human erythrocytes have been studied at 37 degrees C. Previous studies of the enzyme from several mammalian sources, which used a lower assay temperature, have been difficult to interpret because of the substrate activation by acetaldehyde which led to complex kinetic behaviour. At 37 degrees C the initial-rate data do not depart significantly from Michaelis-Menten kinetics. Studies of the variation of initial rates as a function of the concentrations of both substrates and studies of the inhibition by NADH were consistent with a sequential mechanism being followed. High-substrate inhibition by acetaldehyde was competitive with respect to NAD+. The enzyme was not inhibited by the product acetate and thus the results of these studies, although consistent with an ordered mechanism in which NAD+ was the first substrate to bind, were inconclusive. That such a mechanism was followed was confirmed by determination of the initial-rate behaviour in the presence of acetaldehyde and glycolaldehyde as alternative substrates. When the reciprocal of the initial rate of NADH formation was plotted against the acetaldehyde concentration at a series of fixed ratios between that substrate and glycolaldehyde, a linear ‘mixed inhibition’ pattern was obtained, confirming the mechanism to be ordered with NAD+ being the leading substrate and with kinetically significant ternary complex-formation.

Steady-state kinetics of valproic acid in epileptic patients

1978 ◽  
Vol 24 (3) ◽  
pp. 324-332 ◽  
Author(s):  
J. Bruni ◽  
B. J. Wilder ◽  
L. J. Willmore ◽  
R. J. Perchalski ◽  
H. J. Villarreal
Keyword(s):  
Valproic Acid ◽  
Steady State ◽  
Steady State Kinetics ◽  
Epileptic Patients ◽  
Kinetics Of
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