作者: John R. Sheppard , Peter Albersheim , Gerald McClearn
DOI: 10.1016/S0021-9258(18)63070-4
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摘要: Abstract The aldehyde dehydrogenases from livers of the inbred mouse strains C57BL/6J, DBA/2J, and F1 generation cross between these (C57BL/6J x DBA/2J) have been purified over 60-fold. Alcohol dehydrogenase activity is not present in enzyme preparation. Enzyme preparations both specifically require NAD but can oxidize a variety substrates. Results obtained previously, using crude liver homogenate as source indoleacetaldehyde substrate, demonstrate 2- to 3-fold greater aldehyde-oxidizing capacity extracts C57BL/6J strain compared similar DBA/2J mice. Mice former prefer 10% solution alcohol water, whereas mice avoid this preference test. are intermediate parents with regard capacity. enzymes two sources indistinguishable determined by disc gel electrophoresis, ion exchange chromatography, filtration criteria. Nevertheless, exhibit differences Michaelis constants Reaction velocity particularly apparent when acetaldehyde substrate. activated 10-6 m reaction than 2 times its original value, exhibits substrate activation only above 10-3 acetaldehyde. Finally, it has demonstrated chromatographic analysis that, following intraperitoneal ethanol injection, accumulates blood extent does This observation lends support possibility that lower results an acetaldehyde-induced avoidance ethanol.