Results 191 to 200 of about 66,025 (242)
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Distribution of Messenger RNAs for Aldehyde Dehydrogenase 1, Aldehyde Dehydrogenase 2, and Aldehyde Dehydrogenase 5 in Human Tissues

Journal of Investigative Medicine, 1996
Background The distribution of aldehyde dehydrogenases in human tissues is incompletely understood, in part because of technical limitations of gel electrophoretic and other enzyme assay methods used previously and because of the instability of the enzymes.
M J, Stewart, K, Malek, D W, Crabb
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Drosophila melanogaster aldehyde dehydrogenase

Experientia, 1985
Subcellular fractionation by differential centrifugation confirms the presence of aldehyde dehydrogenase in D. melanogaster. It is found principally in the heavy mitochondrial fraction.
M C, Liétaert   +3 more
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Aldehyde Dehydrogenase in Alcoholic Subjects

Hepatology, 1985
Hepatic aldehyde dehydrogenase activity is depressed in alcoholic liver disease and may account for the observation that alcoholics develop high blood acetaldehyde concentrations following ethanol. To determine whether this is a specific defect in alcoholics, aldehyde dehydrogenase was studied in liver tissue obtained from ...
K R, Palmer, W J, Jenkins
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Pharmacogenetics of aldehyde dehydrogenase (ALDH)

Pharmacology & Therapeutics, 1990
Cette synthese aborde le metabolisme des aldehydes chez l'homme et les mammiferes, et en particulier le role de l'aldehyde deshydrogenase. Sont decrits les proprietes physicochimiques de l'enzyme, son expression genique, ses variants genetiques, son importance ...
H W, Goedde, D P, Agarwal
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Betaine aldehyde dehydrogenase in plants

Plant Biology, 2009
AbstractPlant betaine aldehyde dehydrogenases (BADHs) have been the target of substantial research, especially during the last 20 years. Initial characterisation of BADH as an enzyme involved in the production of glycine betaine (GB) has led to detailed studies of the role of BADH in the response of plants to abiotic stressin vivo, and the potential ...
Fitzgerald, Timothy L   +2 more
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Aldehyde Dehydrogenases in Rat Liver

Canadian Journal of Biochemistry, 1972
Two enzymes (I and II) with NAD+-dependent aldehyde dehydrogenase activity have been separated and partially purified from the supernatant fraction of rat liver. Resolution was effected by DEAE-cellulose column chromatography. In addition to the differences in charge properties, these two proteins differ in substrate specificity, that of enzyme II ...
G T, Shum, A H, Blair
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Metabolism of Cyclophosphamide by Aldehyde Dehydrogenases

1995
Cyclophosphamide (Endoxan) and other oxazaphosphorines such as 4-hydroperoxy-cyclophosphamide, ifosfamide, and mafosfamide are widely used as antineoplastic drugs (Sladek, 1988; Lindahl, 1992). The cytotoxic effect is caused by alkylation reaction of these drugs with DNA and proteins inhibiting the cell proliferation.
D P, Agarwal   +3 more
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Metabolic Role of Aldehyde Dehydrogenase

1993
Aldehyde dehydrogenase (EC 1.2.1.3), an enzyme with a broad substrate specificity and low Km values for short chain aliphatic aldehydes utilizes NAD as coenzyme, is universally distributed in mammalian livers and also at lower concentrations in other organs. The enzyme is a homotetramer of MW of ca. 220,000 (see review by Pietruszko, 1989).
W, Ambroziak, R, Pietruszko
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Alcohol dehydrogenases and aldehyde dehydrogenases

Biochemical Society Transactions, 1988
HANS JÖRNVALL   +6 more
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Aldehyde Dehydrogenases and Their Role in Carcinogenesis

Critical Reviews in Biochemistry and Molecular Biology, 1992
Aldehydes are highly reactive molecules that may have a variety of effects on biological systems. They can be generated from a virtually limitless number of endogenous and exogenous sources. Although some aldehyde-mediated effects such as vision are beneficial, many effects are deleterious, including cytotoxicity, mutagenicity, and carcinogenicity.
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