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Keywords: Aldehyde dehydrogenase
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Enzyme (1987) 37 (1-2): 5–18.
Published Online: 11 August 2017
... and repeated isozyme evolution, a subject where alcohol dehydrogenases exceptionally well offer detailed examples. Human aldehyde dehydrogenase occurs of two types, a mitochondrial and a cytosolic form. The enzymes are tetramers, do not contain functional metals, and have subunits which do not form inter-type...
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Enzyme (1985) 33 (3): 153–161.
Published Online: 11 August 2017
...D. Meier-Tackmann; G.C. Korenke; D.P. Agarwal; H.W. Goedde Freshly obtained human term placentae were subjected to subcellular fractionation to study the localization of NAD-dependent aldehyde dehydrogenases. Optimal conditions for the cross-contamination-free subcellular fractionation were...
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Enzyme (1980) 25 (4): 281–286.
Published Online: 11 August 2017
...H. Werner Goedde; Dharam P. Agarwal; Shoji Harada Human liver alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH)play an important role in alcohol metabolism. It has been shown that both enzymes are polymorphic and that different variants may be responsible for individual and racial...
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Enzyme (1975) 19 (2): 85.
Published Online: 11 August 2017
...Fritz Heinz; Friederike Schlegel; Peter H. Krause Activities of enzymes involved in fructose metabolism were measured in samples of human kidney cortex and medulla. The enzymes are ketohexokinase, aldolase,NAD- and NADP-dependent alcohol dehydrogenase, aldehyde dehydrogenase, triokinase...
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Enzyme (1975) 19 (2): 93–101.
Published Online: 11 August 2017
... region and ileum in the region of the valvula ileo coecalis. Ketohexokinase,aldolase, alcohol dehydrogenases NAD- and NADPdependent were found in all gut sections. The activity of aldehyde dehydrogenase was low in all sections tested. Triokinase could be found only in the duodenum and jejunum region...
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Enzyme (1991) 45 (4): 188–193.
Published Online: 11 August 2017
...M.J.C. Crabbe; S.T. Hoe Human lens was found to contain aldehyde dehydrogenase at a level of activity similar to that of bovine lens, namely 1.76 ± 0.51 IU/g. The enzyme, which appears to be a tetramer of 229 kD, was less susceptible to inhibition by cataractogenic agents than the bovine enzyme...
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Enzyme and Protein (1992) 46 (4-5): 239–244.
Published Online: 11 August 2017
...Akira Yoshida; Lily C. Hsu; Vibha Davé The major cytosolic aldehyde dehydrogenase isozyme (ALDH1) exhibits strong activity for oxidation of retinal to retinoic acid, while the major mitochondrial ALDH2 and the stomach cytosolic ALDH3 have no such activity. The K(m) of ALDH1 for retinal is about...