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Abstract
Leucine aminopeptidase IV in extracts of wheat bran culture of Aspergillus oryzae 460 was separated from arylamidase by polyacrylamide gel disc electrophoresis at pH 8.0 for 1 hr. The purified enzyme showed neither arylamidase nor amidase activity. The optimum pH was 7.0 on l-leucyl-l-glycyl-l-glycine (Leu-Gly-Gly) as substrate. The enzyme was inhibited by diisopropylphosphorofluoridate (DFP), but not by metal chelating agents. The enzyme molecular weight was estimated to be about 130,000 by gel filtration method.