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The inactivation of the affinity chromatography purified low-Km rat liver mitochondrial aldehyde dehydrogenase (ALDH)--free of catalase activity--by the alcohol sensitizing agent cyanamide was studied in vitro. This ALDH-purified preparation was not susceptible to cyanamide inactivation at concentrations up to 2.5 mM. On the other hand, ALDH activity appears to be irreversibly inhibited when the incubation mixture contained ALDH, catalase, NAD+ and cyanamide. Influence of catalase, NAD+ and cyanamide concentrations in the incubation mixtures on the ALDH activity were also established. The time course of the concentration of cyanamide in an incubation mixture when ALDH activity was inhibited by cyanamide in the presence of catalase and NAD+, was evaluated by HPLC. No disappearance of cyanamide was observed for a period of time up to 24 hr. This result suggests that no metabolic conversion of cyanamide to an active inhibitory form takes place, as has been suggested recently.
J Pruńonosa, and
M L Sagristá, and
J Bozal
January 1991,
Drug metabolism and disposition: the biological fate of chemicals,
J Pruńonosa, and
M L Sagristá, and
J Bozal
April 1985,
Biochemical pharmacology,
J Pruńonosa, and
M L Sagristá, and
J Bozal
July 1983,
Biochemical pharmacology,
J Pruńonosa, and
M L Sagristá, and
J Bozal
January 1985,
Alcohol (Fayetteville, N.Y.),
J Pruńonosa, and
M L Sagristá, and
J Bozal
September 1991,
Biochemical pharmacology,
J Pruńonosa, and
M L Sagristá, and
J Bozal
January 1995,
Biochemical pharmacology,
J Pruńonosa, and
M L Sagristá, and
J Bozal
April 1994,
Biochemical pharmacology,
J Pruńonosa, and
M L Sagristá, and
J Bozal
December 1992,
Alcoholism, clinical and experimental research,
J Pruńonosa, and
M L Sagristá, and
J Bozal
January 1990,
Alcohol (Fayetteville, N.Y.),
J Pruńonosa, and
M L Sagristá, and
J Bozal
December 1976,
Biochemical pharmacology,
