Abstract
An assay for lipoxidase in animal tissues has been developed which eliminates the interference of heme compounds. Catalytic oxidation of linoleate emulsions at pH 9.0 by heme pigments was inhibited by potassium cyanide while lipoxidase activity was relatively unaffected. The assay method was capable of detecting extremely low levels of lipoxidase activity in animal tissue. Application of the method to beef and pork adipose tissue, uncured bacon, cured unsmoked bacon, and rabbit liver, kidney, spleen, heart, brain, and lung strongly suggested that lipoxidase was not present in these tissues and that the linoleate oxidation was catalyzed by the heme pigments in the extracts.
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