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Reduction of polyunsaturated fatty acid hydroperoxides by human brain glutathione peroxidase
Author(s) -
Kaplan E.,
Ansari K.
Publication year - 1984
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02534472
Subject(s) - polyunsaturated fatty acid , chemistry , arachidonic acid , biochemistry , glutathione , glutathione peroxidase , peroxidase , linoleic acid , linolenic acid , clinical chemistry , fatty acid , enzyme , chromatography
Glutathione peroxidase (GSHPx) activity in the normal human brain was investigated using lipid hydroperoxides as substrates. Samples were obtained from autopsied frontal gray matter of 5 normal human males with no known central nervous system (CNS) disease. Aliquots were homogenized in 0.9% NaCl‐0.5% Triton X‐100, and the supernatant solution, obtained after centrifugation at 105,000 × g, was used for GSHPx assay. Glutathione peroxidase was measured by following the oxidation of NADPH at 340 nm. Hydroperoxides of linoleic, linolenic, gamma linolenic, 11,14 eicosodienoic, homo gamma linolenic, arachidonic, docosotetraenoic and docosohexaenoic acids were prepared and used as substrates. All these hydroperoxides were reduced by the brain GSHPx system, but at different rates. Gamma linolenic and docosotetraenoic hydroperoxides were reduced rapidly, whereas the peroxides of docosohexaenoic and 11,14 eicosodienoic were reduced at the lowest rate. Arachidonic hydroperoxide had the highest affinity for the enzyme and linolenic the lowest. Our results suggest that the brain GSHPx system is capable of reducing hydroperoxides of polyunsaturated fatty acids.