Characterization of prolidase I and II from erythrocytes of a control, a patient with prolidase deficiency and her mother

Toshitaka Oohashi, Takashi Oono, Jiro Arata, Kazunobu Sugahara, Hiroyuki Kodama

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Prolidase I (EC 3.4.13.9) was purified to homogeneity from the erythrocytes of a normal human (control) and the patient's mother, and prolidase II from erythrocytes of a control and the patient's mother, and prolidase from the patient's erythrocytes was also highly purified. The various properties of the patient's prolidase were compared to those of prolidase from a control and the patient's mother. Prolidase I from a control and the patient's mother had a molecular weight of about 112,000, and was composed of two subunits with an identical molecular weight of 56,000. The Km values for Gly-Pro of the control's and the patient's mother's prolidase I were 2.90 ± 0.22 and 2.88 ± 0.27 mM, but the Vmax values for Gly-Pro of the mother's enzyme was reduced about 30% compared to that of control enzymes (mother: 6.02 units/mg protein, control: 22.21 units/mg protein). Isoionic points of these enzymes by chromatofocusing were pH 4.6 $ ̃4.7. Prolidase II from the control and the patient's mother, and the patient's prolidase had a molecular weight of about 185,000, and was composed of two subunits with an identical molecular weight of 95,000. The Km and Vmax values for various substrates of prolidase II from a control and the patient's mother, and the patient's prolidase were almost the same.

Original languageEnglish
Pages (from-to)1-9
Number of pages9
JournalClinica Chimica Acta
Volume187
Issue number1
DOIs
Publication statusPublished - Jan 31 1990
Externally publishedYes

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proline dipeptidase
Prolidase Deficiency
Erythrocytes
Mothers
Molecular weight
glycylproline
Molecular Weight
Enzymes

Keywords

  • Erythrocyte
  • Prolidase
  • Prolidase deficiency

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry

Cite this

Characterization of prolidase I and II from erythrocytes of a control, a patient with prolidase deficiency and her mother. / Oohashi, Toshitaka; Oono, Takashi; Arata, Jiro; Sugahara, Kazunobu; Kodama, Hiroyuki.

In: Clinica Chimica Acta, Vol. 187, No. 1, 31.01.1990, p. 1-9.

Research output: Contribution to journalArticle

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AB - Prolidase I (EC 3.4.13.9) was purified to homogeneity from the erythrocytes of a normal human (control) and the patient's mother, and prolidase II from erythrocytes of a control and the patient's mother, and prolidase from the patient's erythrocytes was also highly purified. The various properties of the patient's prolidase were compared to those of prolidase from a control and the patient's mother. Prolidase I from a control and the patient's mother had a molecular weight of about 112,000, and was composed of two subunits with an identical molecular weight of 56,000. The Km values for Gly-Pro of the control's and the patient's mother's prolidase I were 2.90 ± 0.22 and 2.88 ± 0.27 mM, but the Vmax values for Gly-Pro of the mother's enzyme was reduced about 30% compared to that of control enzymes (mother: 6.02 units/mg protein, control: 22.21 units/mg protein). Isoionic points of these enzymes by chromatofocusing were pH 4.6 $ ̃4.7. Prolidase II from the control and the patient's mother, and the patient's prolidase had a molecular weight of about 185,000, and was composed of two subunits with an identical molecular weight of 95,000. The Km and Vmax values for various substrates of prolidase II from a control and the patient's mother, and the patient's prolidase were almost the same.

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