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Studies on substrate specificity of X-prolyl dipeptidyl-aminopeptidase using new chromogenic substrates, X-Y-p-nitroanilides

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Summary

Substrate specificity of X-prolyl dipeptidyl-aminopeptidase (dipeptidyl aminopeptidase IV) was examined by using newly synthesized 8 chromogenic substrates, X-Y-p-nitroanilides. Homogeneous enzyme from human submaxillary gland hydrolyzed glycylproline p-nitroanilide almost specifically, except alanylalanine p-nitroanilide which had 11% activity.

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Authors and Affiliations

  1. Laboratory of Cell Physiology, Department of Life Chemistry, Graduate School at Nagatsuta, Tokyo Institute of Technology, 227, Yokohama, (Japan)

    T. Kato, T. Nagatsu, T. Kimura & S. Sakakibara

  2. Peptide Institute, Protein Research Foundation, 562, Minoh, Osaka, (Japan)

    T. Kato, T. Nagatsu, T. Kimura & S. Sakakibara

Authors
  1. T. Kato
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  2. T. Nagatsu
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  3. T. Kimura
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  4. S. Sakakibara
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Kato, T., Nagatsu, T., Kimura, T. et al. Studies on substrate specificity of X-prolyl dipeptidyl-aminopeptidase using new chromogenic substrates, X-Y-p-nitroanilides. Experientia 34, 319–320 (1978). https://doi.org/10.1007/BF01923010

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  • DOI: https://doi.org/10.1007/BF01923010

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