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Characterization of prolidase I and II purified from normal human erythrocytes: comparison with prolidase in erythrocytes from a patient with prolidase deficiency

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Abstract

The effect of various sulfur-containing amino acids on the activities of prolidase isoenzymes I and II isolated from erythrocytes of healthy individuals, and erythrocyte lysates from a patient with prolidase deficiency was investigated. The activity of prolidase I against glycylproline was strongly enhanced by d-methionine. l-Methionine and d,l-methionine slightly enhanced the activity at low concentration, but N-acetyl-l-methionine had no effect. d-Ethionine, l-ethionine, and d,l-ethionine also enhanced the activity of prolidase I. d,l-Homocysteine enhanced the activity at low concentration, but inhibited the activity at 50 mM. The activity of prolidase II against methionylproline was enhanced by d-methionine, d,l-methionine, and l-methionine, but N-acetyl-l-methionine had no effect. d-Ethionine and d,l-ethionine strongly enhanced the activity of prolidase II compared with l-ethionine; d,l-homocysteine weakly enhanced the activity. d,l-Homocysteine-thiolactone inhibited the activities of prolidase I and II in a concentration-dependent manner. The effect of various sulfur-containing amino acids on prolidase activity against methionylproline in erythrocyte lysates from a patient with prolidase deficiency was almost the same as that on prolidase II. The kinetics of the activities of prolidase I, II, and patient prolidase were also studied. Their K m values were changed by adding sulfur-containing amino acids, but V max values were unchanged.

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Acknowledgments

We would like to thank Professor Hajime Kodama, Department of Dermatology, Kochi Medical School, for supplying the erythrocytes from a patient with prolidase deficiency.

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Authors and Affiliations

  1. Department of Anesthesiology and Critical Care Medicine, Kochi Medical School, Nankoku-shi, Kochi, 783-8505, Japan

    Soichiro Uramatsu, Gang Liu, Mutsumi Uramatsu, Haidong Chi, Koichi Yamashita & Hiroyuki Kodama

  2. Department of Anesthesiology, First Affiliated Hospital of China Medical University, Nanjing North Road 55, Shenyang, China

    Gang Liu

  3. Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT, 06511, USA

    Qing Yang

  4. Department of Medical Plant Development, Shenyang Pharmaceutical University, No 103 Wenhua Road, Shenyang, China

    Jincai Lu

Authors
  1. Soichiro Uramatsu
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  2. Gang Liu
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  3. Qing Yang
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  4. Mutsumi Uramatsu
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  5. Haidong Chi
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  6. Jincai Lu
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  7. Koichi Yamashita
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  8. Hiroyuki Kodama
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Correspondence to Hiroyuki Kodama.

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Uramatsu, S., Liu, G., Yang, Q. et al. Characterization of prolidase I and II purified from normal human erythrocytes: comparison with prolidase in erythrocytes from a patient with prolidase deficiency. Amino Acids 37, 543–551 (2009). https://doi.org/10.1007/s00726-009-0262-7

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  • DOI: https://doi.org/10.1007/s00726-009-0262-7

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