Reduction of polyunsaturated fatty acid hydroperoxides by human brain glutathione peroxidase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1984-10

AUTHORS

E. Kaplan, K. Ansari

ABSTRACT

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 X 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. More... »

PAGES

784-789

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf02534472

DOI

http://dx.doi.org/10.1007/bf02534472

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1043286740

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/6503623


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