An aminopeptidase from Aspergillus orvzae 460 was purified from the rivanol precipitable fraction. The partially purified enzyme was not homogeneous in disc electrophoresis, although symmetric profiles were obtained for enzyme protein and activity in Sephadex gel filtration.
Acid carboxypeptidase III from Aspergillus oryzae was purified from the rivanol nonprecipitated fraction. The optimum activity of the enzyme occurred at pH 3.0 for carboben zoxy-L-glutamyl-L-tyrosine. The enzyme was inhibited by diisopropylphosphorofluoridate and SH reagents such as p-chloromercuribenzoate and monoiodoacetate, but not by such metal chelating agents as ethylenediaminetetraacetate, ƒ¿,ƒ¿•L-dipyridyl and o-phenanthroline. The
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