PMID: 2510829Nov 17, 1989Paper

Oxygenation of mitochondrial membranes by the reticulocyte lipoxygenase. Action on monoamine oxidase activities A and B

Biochimica Et Biophysica Acta
R WiesnerT Schewe

Abstract

Incubation of isolated rat liver mitochondria with the pure rabbit reticulocyte lipoxygenase caused a time-dependent inactivation of the monoamine oxidase activities A and B. Furthermore, a conversion of the monoamine oxidase into a diamine oxidase was observed. The inactivation kinetics for both monoamine oxidase activities A and B showed a biphasic behaviour; a reversible short-term inhibition during the first 5 min of incubation was followed by an irreversible inactivation of the enzyme. The kinetic studies suggest that the slow irreversible inactivation of the monoamine oxidase activities is due to secondary reactions subsequent to the initial attack of the lipoxygenase on the mitochondrial outer membrane. During the interaction of the lipoxygenase with the mitochondria, only about 1.5% of the polyenoic fatty acids present in the mitochondrial membranes were oxygenated. The predominant products formed during the interaction of the lipoxygenase with the mitochondrial membranes are (13S)-hydro(pero)xy-9Z,11E-octadecadienoic acid and (15S)-hydro(pero)xy-5,8,11,13(Z,Z,Z,E)-eicosatetraenoic acid.

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Citations

Apr 1, 1994·International Journal of Developmental Neuroscience : the Official Journal of the International Society for Developmental Neuroscience·A E Medvedev, V Z Gorkin
Jul 12, 2012·Cellular and Molecular Life Sciences : CMLS·Chi Chiu WangChristoph Ufer
Oct 8, 2004·The Journal of Immunology : Official Journal of the American Association of Immunologists·Pavlos ChaitidisHartmut Kühn

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