Heimann W, Klaiber V
Z Lebensm Unters Forsch. 1977 Dec 9;165(3):140-3. doi: 10.1007/BF01650745.
Oat isomerase is inhibited by hydroxyoctadecadienoic acids (monohydroxy acids) to a degree comparable with inhibition by linoleic acid hydroperoxides (LHPO). Hydroxy acids seem to combine with the enzyme like LHPO do. In an experiment on LHPO breakdown by isomerase 1-14C-hydroxy acids were added and it was examined whether the epoxyhydroxy acids are formed by an intermolecular or intramolecular mechanism. In this experiment 1-14C-labeled trihydroxy acids were formed; they arise from the hydrolysis of epoxyhydroxyoctadecenoic acids formed on their part by isomerase effected LHPO-breakdown. It was determined that at least 70% of LHPO are converted by intermolecular reaction.
