Showing papers on "Aldehyde dehydrogenase published in 1970"
TL;DR: The limited capacity of brain to oxidize aldehydes may be of pharmacological importance because it facilitates the production of tetrahydropapaveroline in the presence of drugs which inhibit this enzyme.
Abstract: Tetrahydropapaveroline is a benzyltetrahydroisoquinoline alkaloidderivative of the biogenic amine, dopnmine. Alcohol, by way of its primary metabolite, acetaldehyde, competitively inhibits nicotinamide-adenine Sinucleotide-linked aldehyde dehydrogenase and augments the formation of tetrahydropapaveroline in vitro. The limited capacity of brain to oxidize aldehydes may be of pharmacological importance because it facilitates the production of tetrahydropapaveroline in the presence of drugs which inhibit this enzyme.
534 citations
TL;DR: It has been demonstrated by chromatographic analysis that, following intraperitoneal ethanol injection, acetaldehyde accumulates in the blood of DBA/2J mice to a greater extent than it does in C57BL/6J mice, lending support to the possibility that the lower aldehyde dehydrogenase activity of the DBA or 2J mice results in an acetaldehyde-induced avoidance of ethanol.
142 citations
TL;DR: By avoiding autolysis and using large concentrations of the esterase inhibitors, diisopropyl fluorophosphate and phenylmethylsulfonylfluoride, the enzyme was isolated in a 10-fold greater yield and in a form in which serine was the amino-terminal end group.
55 citations
TL;DR: Kinetics properties and particularly the variation of the Km and νmax as a function of chain length of the substrates are reported and alkane and the corresponding alcohol and aldehyde are inducers of these enzymes.
48 citations
Journal Article•
TL;DR: The findings suggest that the antialcohol action of butyraldoxime in C57BL mice and in man is probably derived from hepatic aldehyde dehydrogenase blockade which interferes with the metabolism of acetaldehyde derived from ethanol.
Abstract: Simultaneous consumption of butyraldoxime and ethanol induced a strong and protracted decrease in ethanol preference in C57BL mice, a strain with natural preference for ethanol solutions. Biochemical studies showed that butyraldoxime is a potent inhibitor of hepatic alcohol dehydrogenase in vitro and in vivo in rodents. Intraperitoneal treatment resulted in decreased activity of liver extracts, delayed disappearance of blood ethanol after an ethanol dose and reduced accumulation of citric acid in kidney elicited by fluoroethanol. The lack of in vitro inhibition of hepatic aldehyde dehydrogenase was confirmed; however, butyraldoxime is a strong inhibitor of aldehyde dehydrogenase in vivo . Intraperitoneal treatment resulted in decreased activity of liver extracts and acetaldehyde accumulation in blood after an ethanol dose. After chronic intake of butyraldoxime in the drinking fluid, mice and rats also showed markedly decreased aldehyde dehydrogenase activity but slightly enhanced alcohol dehydrogenase activity. Subsequent administration of ethanol resulted in the appearance of substantial amounts of acetaldehyde in blood and a slightly slower rate of disappearance of ethanol from blood. These findings suggest that the antialcohol action of butyraldoxime in C57BL mice and in man is probably derived from hepatic aldehyde dehydrogenase blockade which interferes with the metabolism of acetaldehyde derived from ethanol. Analogous effects on ethanol metabolism were also found for several homologous aldoximes.
21 citations
TL;DR: Dissociation and reassociation of one of the hybrid forms resulted in the formation principally of a catalytically active aldehyde dehydrogenase, indistinguishable from the native enzyme.
18 citations
Journal Article•
16 citations
4 citations
TL;DR: Results indicated that carbohydrate metabolism in the organism follows both Embden-Meyerhof-Parnas and Hexose monophosphate shunt pathways.
Abstract: Streptococcus lactis possessed glucose-6-phosphate-dehydrogenase, 6-phosphogluconic-dehydrogenase, ribose-5-phosphate isomerase and transketolase enzyme activities. The presence of the previously reported aldolase, lactic dehydrogenase, alcohol dehydrogenase and aldehyde dehydrogenase activities in the organism was confirmed. These results indicated that carbohydrate metabolism in the organism follows both Embden-Meyerhof-Parnas and Hexose monophosphate shunt pathways. The presence of aldolase, glucose-6-phosphate-dehydrogenase and 6-phosphogluconic-dehydrogenase is in accordance with the fact that the organism is a facultative homofermenter.
2 citations