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A spectrophotometric assay for hydroperoxide lyase

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Lipids

Abstract

Spectrophotometric assays for hydroperoxide lyase have traditionally measured the loss in absorption at 234 nm due to the disruption of conjugated diene in the fatty acid hydroperoxide. However, that assay does not distinguish between hydroperoxide lyase and hydroperoxide dehydrase activities, both of which cause a loss of conjugation in the substrate hydroperoxide. A new assay has been developed which is specific for hydroperoxide lyase. It is based on the ability of hydroperoxide lyase products, aldehydes and ω-oxoacids, to serve as substrates for yeast alcohol dehydrogenase. Thus, the new hydroperoxide lyase assay is a coupled enzyme assay, which is conducted spectrophotometrically at 340 nm and measures the oxidation of nicotinamide adenenine dinucleotide, reduced form (NADH). In addition to its specificity for hydroperoxide lyase, the coupled assay allows higher concentrations of both fatty acid hydroperoxide substrate and crude enzyme extracts than the assay conducted at 234 nm.

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Abbreviations

ADH:

alochol dehydrogenase

NADH:

nicotinamide adenenine dinucleotide, reduced form.

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Authors and Affiliations

  1. Agricultural Research Service, Northern Crop Science Laboratory, U.S. Department of Agriculture, P.O. Box 5677, 58105, Fargo, North Dakota

    Brady A. Vick

Authors
  1. Brady A. Vick
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Names of products are included for the benefit of the reader and do not imply endorsement or preferential treatment by the United States Department of Agriculture.

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Vick, B.A. A spectrophotometric assay for hydroperoxide lyase. Lipids 26, 315–320 (1991). https://doi.org/10.1007/BF02537143

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  • DOI: https://doi.org/10.1007/BF02537143

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