Purification and characterization of an enkephalin-degrading aminopeptidase from guinea pig serum |
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Authors: | Mariko Shimamura Tadahiko Hazato Takashi Katayama |
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Institution: | Department of Medical Chemistry, The Tokyo Metropolitan, Institute of Medical Science, Honkomagome, Bunkyo-ku, Tokyo 113, Japan |
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Abstract: | An enkaphalin-degrading aminopeptidase using Leu-enkephalin as a substrate was purified about 4100-fold from guinea pig serum. The purified preparation was apparently homogenous, showing on polyacrylamide gel electrophoresis. The molecular weight of the enzyme was approx. 92 000. The amino-peptidase had a pH optimum of 7.0 with Km values of 0.12 mM and 0.18 mM for Leu- and Met-enkephalin, respectively. The enzyme hydrolyzed neutral, basic and aromatic amino acid β-naphthylamides, but did not the acidic one. The enzyme was inhibited strongly by metal-chelating agents, bestatin and amastatin and weakly by puromycin. Among several biologically active peptides, angiotensin III and substance P strongly inhibited the enzyme. |
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Keywords: | Enkephalin degradation Aminopeptidase (Guinea pig serum) |
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