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Purification and Properties of Acid Carboxypeptidase IV from Aspergillus oryzae
Authors:Tadanobu Nakadai  Seiichi Nasuno  Nobuyoshi Iguchi
Affiliation:Noda Institute for Scientific Research, Noda-shi, Chiba-ken
Abstract:
Acid carboxypeptidase IV from Aspergillus oryzae was purified from the rivanol precipitable fraction by column chromatography on DEAE-cellulose, DEAE-Sephadex A–50, hydroxylapatite and P-cellulose and gel filtration through Sephadex G–100. The optimum pH is at pH 3.0 for carbobenzoxy-l-glutamyl-l-tyrosine. The enzyme activity was inhibited by sulfhydryl reagents and diisopropylphosphorofluoridate, but was not inhibited by metal chelating agents. The molecular weight of the enzyme was estimated to be about 43,000 by gel filtration method.
Keywords:L-carnitine dehydrogenase  C-terminal region  Xanthomonas  Rhizobium
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