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A new acid carboxypeptidase, O-1, fromAspergillus oryzae

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Abstract

A new acid carboxypeptidase was purified fromAspergillus oryzae grown on solid bran culture medium. The purified enzyme was found to be homogeneous by disc gel electrophoresis at pH 9.4 and isoelectric focusing. The enzyme was termedA. oryzae acid carboxypeptidase O-1 with isoelectric point 4.08. The substrate specificity of the new enzyme was investigated with proangiotensin, angiotensin, and bradykinin. Even when the proline was present at the penultimate position of the peptide, the enzyme rapidly hydrolyzed the carboxyterminal Pro-X (X=amino acid) peptide bond. TheK m andk cat values for angiotension (−Pro7−Phe8) at pH 3.7 and 30°C were 0.2 mM and 1.7 sec−1, respectively.

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Authors and Affiliations

  1. Laboratory of Enzymology and Microbial Chemistry, Tokyo Nōkō University, 183, Fuchu, Tokyo, Japan

    Michio Takeuchi, Taro Ushijima & Eiji Ichishima

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  1. Michio Takeuchi
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  2. Taro Ushijima
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  3. Eiji Ichishima
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Takeuchi, M., Ushijima, T. & Ichishima, E. A new acid carboxypeptidase, O-1, fromAspergillus oryzae . Current Microbiology 7, 19–23 (1982). https://doi.org/10.1007/BF01570974

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