P D Buckley - JoVE Visualize

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The Biochemical Journal|June 1, 1978

Steady-state and pre-steady kinetic studies on mitochondrial sheep liver aldehyde dehydrogenase. A comparison with the cytoplasmic enzymeA K MacGibbon, L F Blackwell, P D Buckley

Biological Trace Element Research|January 1, 1992

Glucose tolerance factor potentiation of insulin action in adipocytes from rats raised on a torula yeast diet cannot be attributed to a deficiency of chromium or glucose tolerance factor activity in the dietP R Shepherd, C Elwood, P D Buckley, et al.

Biochemistry|February 27, 1990

Evidence for reactivity of serine-74 with trans-4-(N,N-dimethylamino)cinnamaldehyde during oxidation by the cytoplasmic aldehyde dehydrogenase from sheep liverK M Loomes, G G Midwinter, L F Blackwell, et al.

Archives of Biochemistry and Biophysics|December 1, 1985

Kinetics of inhibition and hysteresis of sheep liver cytoplasmic aldehyde dehydrogenase with glyoxylic acid: further evidence relating to the two-site model for aldehyde oxidationL W Deady, P D Buckley, A F Bennett, et al.

The Biochemical Journal|September 15, 1988

Evidence that the cytoplasmic aldehyde dehydrogenase-catalysed oxidation of aldehydes involves a different active-site group from that which catalyses the hydrolysis of 4-nitrophenyl acetateR L Motion, P D Buckley, A F Bennett, et al.

Archives of Biochemistry and Biophysics|April 1, 1994

The effect of p-(chloromercuri)benzoate modification of cytosolic aldehyde dehydrogenase from sheep liver. Evidence for a second aldehyde binding siteJ P Hill, R L Motion, P D Buckley, et al.

Biochemistry|February 5, 1991

Steady-state and pre-steady-state kinetics of propionaldehyde oxidation by sheep liver cytosolic aldehyde dehydrogenase at pH 5.2. Evidence that the release of NADH remains rate-limiting in the enzyme mechanism at acid pH valuesJ P Hill, L F Blackwell, P D Buckley, et al.

The Biochemical Journal|February 1, 1991

Effect of pyrophosphate ions and alkaline pH on the kinetics of propionaldehyde oxidation by sheep liver cytosolic aldehyde dehydrogenaseJ P Hill, P D Buckley, L F Blackwell, et al.

The Biochemical Journal|June 1, 1978

Kinetic studies on the esterase activity of cytoplasmic sheep liver aldehyde dehydrogenaseA K MacGibbon, S J Haylock, P D Buckley, et al.

The Biochemical Journal|March 15, 1987

Evidence that the slow conformation change controlling NADH release from the enzyme is rate-limiting during the oxidation of propionaldehyde by aldehyde dehydrogenaseL F Blackwell, R L Motion, A K MacGibbon, et al.

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Showing results (11-20 of 26) with videos related to

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The Biochemical Journal|June 1, 1978

Steady-state and pre-steady kinetic studies on mitochondrial sheep liver aldehyde dehydrogenase. A comparison with the cytoplasmic enzymeA K MacGibbon, L F Blackwell, P D Buckley

Biological Trace Element Research|January 1, 1992

Glucose tolerance factor potentiation of insulin action in adipocytes from rats raised on a torula yeast diet cannot be attributed to a deficiency of chromium or glucose tolerance factor activity in the dietP R Shepherd, C Elwood, P D Buckley, et al.

Biochemistry|February 27, 1990

Evidence for reactivity of serine-74 with trans-4-(N,N-dimethylamino)cinnamaldehyde during oxidation by the cytoplasmic aldehyde dehydrogenase from sheep liverK M Loomes, G G Midwinter, L F Blackwell, et al.

Archives of Biochemistry and Biophysics|December 1, 1985

Kinetics of inhibition and hysteresis of sheep liver cytoplasmic aldehyde dehydrogenase with glyoxylic acid: further evidence relating to the two-site model for aldehyde oxidationL W Deady, P D Buckley, A F Bennett, et al.

The Biochemical Journal|September 15, 1988

Evidence that the cytoplasmic aldehyde dehydrogenase-catalysed oxidation of aldehydes involves a different active-site group from that which catalyses the hydrolysis of 4-nitrophenyl acetateR L Motion, P D Buckley, A F Bennett, et al.

Archives of Biochemistry and Biophysics|April 1, 1994

The effect of p-(chloromercuri)benzoate modification of cytosolic aldehyde dehydrogenase from sheep liver. Evidence for a second aldehyde binding siteJ P Hill, R L Motion, P D Buckley, et al.

Biochemistry|February 5, 1991

Steady-state and pre-steady-state kinetics of propionaldehyde oxidation by sheep liver cytosolic aldehyde dehydrogenase at pH 5.2. Evidence that the release of NADH remains rate-limiting in the enzyme mechanism at acid pH valuesJ P Hill, L F Blackwell, P D Buckley, et al.

The Biochemical Journal|February 1, 1991

Effect of pyrophosphate ions and alkaline pH on the kinetics of propionaldehyde oxidation by sheep liver cytosolic aldehyde dehydrogenaseJ P Hill, P D Buckley, L F Blackwell, et al.

The Biochemical Journal|June 1, 1978

Kinetic studies on the esterase activity of cytoplasmic sheep liver aldehyde dehydrogenaseA K MacGibbon, S J Haylock, P D Buckley, et al.

The Biochemical Journal|March 15, 1987

Evidence that the slow conformation change controlling NADH release from the enzyme is rate-limiting during the oxidation of propionaldehyde by aldehyde dehydrogenaseL F Blackwell, R L Motion, A K MacGibbon, et al.

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