Inhibition of 5‐lipoxygenase by vitamin E
- 12 November 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 193 (1), 39-43
- https://doi.org/10.1016/0014-5793(85)80075-2
Abstract
Purified 5-lipoxygenase from potato tubers was inhibited strongly by vitamin E and its analogs. The inhibition by d-alpha-tocopherol was found to be irreversible and non-competitive with respect to arachidonic acid. An IC50 of 5 microM was calculated for d-alpha-tocopherol. The inhibition appears to be unrelated to its antioxidant function. Binding studies with 14C-labelled d-alpha-tocopherol revealed that there is a strong interaction between vitamin E and 5-lipoxygenase. Tryptic digestion and peptide mapping of 5-lipoxygenase-vitamin E complex indicate that vitamin E binds strongly to a single peptide. These studies suggest that cellular vitamin E levels may have profound influence on the formation of leukotrienes.This publication has 7 references indexed in Scilit:
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