On the role of microsomal aldehyde dehydrogenase in metabolism of aldehydic products of lipid peroxidation.
To elucidate a possible role of membrane-bound aldehyde dehydrogenase in the detoxication of aldehydic products of lipid peroxidation, the substrate specificity of the highly purified microsomal enzyme was investigated. The aldehyde dehydrogenase was active with different aliphatic aldehydes including 4-hydroxyalkenals, but did not react with malonic dialdehyde. When Fe/ADP-ascorbate-induced lipid peroxidation of arachidonic acid was carried out in an in vitro system, the formation of products which react with microsomal aldehyde dehydrogenase was observed parallel with malonic dialdehyde accumulation.
All-Union Research Center for Medico-Biological Problems of Narcology, Moscow, USSR.
V D
VD
Antonenkov
S V
SV
Pirozhkov
L F
LF
Panchenko
D000444:Aldehyde Dehydrogenase / Q000378:metabolism*; D000818:Animals; D007700:Kinetics; D008054:Lipid Peroxides / Q000378:metabolism*; D008566:Membranes / Q000201:enzymology; D008862:Microsomes, Liver / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D051381:Rats; D012995:Solubility; D013379:Substrate Specificity
D008054:Lipid Peroxides; D009243:NAD; D000444:Aldehyde Dehydrogenase