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Inhibition of 5‐lipoxygenase by vitamin E
Author(s) -
Reddanna Pallu,
Krishna Rao M.,
Channa Reddy C.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80075-2
Subject(s) - lipoxygenase , chemistry , vitamin , biochemistry , enzyme
Purified 5‐lipoxygenase from potato tubers was inhibited strongly by vitamin E and its analogs. The inhibition by d‐α‐tocopherol was found to be irreversible and non‐competitive with respect to arachidonic acid. An IC 50 of 5μM was calculated for d‐α‐tocopherol. The inhibition appears to be unrelated to its antioxidant function. Binding studies with 14 C‐labelled d‐α‐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.