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Abstract
Pepsin was activated by incubating with linoleic acid hydroperoxides (LAHPO) at acidic region except at pH 4.0. Especially, the activation was best in pH 5.0 and 6.0 buffers, and the maximum activity attained was about 2 times of the original. It is still not certain whether LAHPO combined to the protein molecule or hydroperoxide groups reacted with some special amino acid residues in the protein molecule. The reactions were very sensitive to pH change and some conformational change of the protein molecule may be involved.