Sheep liver cytosolic aldehyde dehydrogenase : a fresh perspective : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science in Chemistry at Massey University, New Zealand
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Date
1995
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Massey University
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Abstract
The pre-steady-state mechanism of aldehyde dehydrogenase has been further investigated using synthesised deuterated 4-trans-(N,N-dimethylamino) cinnamaldehyde as a substrate. Reporter groups of the active site of ALDH have indicated the presence of a divalent or trivalent metal electrophile, shown in chapter 3 as being either Fe
(II)
or Fe
(III)
. Studies of the spectral properties of NADH bound to aldehyde dehydrogenase have revealed the presence of at least two spectrally different enzyme-NADH species. The consequences of this information are important in interpretation of the kinetic data and understanding apparently contradictory experimental results from different research workers. The steady-state kinetics of ALDH have been further investigated. A sensitive substrate for use in enzyme immunoassays has been designed and synthesised. The preliminary kinetic behaviour observed using this substrate has been studied with three enzymes. Aldehyde dehydrogenase has been used as a model system for studying the effects of electromagnetic radiation on biological systems.
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Keywords
Aldehyde dehydrogenase, Alcohol metabolism