Role of the Intracellular Distribution of Hepatic Catalase in the Peroxidative Oxidation of Methanol
Year: 1969
Type: article
Abstract: Previous to 1950, when Bonnichsenl isolated crystalline alcohol dehydrogenase (ADH) and showed that it did not react with methanol,$ it was believed that the ADH system was responsible for the oxidation of all primary aliphatic alcohols, including methanol (FIGURE 1 ) .This observation redirected attention to the peroxidative system as a means of oxidizing methanol.As early as 1936, Keilin and Hartree3 showed that catalase catalyzed the oxidation of alcohols to their aldehydes when hydrogen peroxide was supplied in low concentrations, as might be provided in living cells through the action of flavin and other peroxide-generating enzymes.They presented arguments to support their view that catalase is not present in the tissues to protect against peroxide intoxication, as was widely contended, but rather to carry out coupled (peroxidative) oxidations.Employing techniques that permitted very rapid spectral determinations, Chance4 identified the intermediate complexes and analyzed the kinetics of the components of the reaction (FIGURE 1 ) .Ideas were exchanged for several years as to whether or not the peroxidative system participated in the in vivo oxidation of methanol and other alcohols.A direct means of examining the question was provided when Heim and coworkers5 showed that the intraperitoneal injection of 3-amino-1,2,4-triazole (AT) caused a reduction in hepatic and renal catalase activities of 90% or more.Mannering and Parkss found that the AT-induced inhibition of hepatic catalase was accompanied by a 70% reduction of the methanol-oxidizing capacity of rat liver homogenates.
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2139972268