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Journal of Inherited Metabolic Disease

, Volume 12, Issue 4, pp 379–385 | Cite as

Biochemical nature of pyruvate dehydrogenase complex in the patient with primary lactic acidaemia

  • A. Kitano
  • F. Endo
  • Y. Kuroda
  • S. Aso
  • T. Kawasaki
  • I. Matsuda
Article

Summary

The biochemical nature of the pyruvate dehydrogenase complex (PDHC) in muscle was studied in a patient with pyruvate dehydrogenase complex deficiency. The enzyme activity was approximately 30% of the control level and the apparentKm value of the enzyme was similar to the control value. The immunoblot pattern of each subunit protein, E, E, the component X, E2 and E3, was comparable to that of the control on both one-and two-dimensional electrophoresis, the staining of each subunit protein being reduced in intensity, corresponding to the reduced enzyme activity. The enzyme deficiency is likely to be quantitative rather than qualitative, although the actual mechanism is unknown.

Keywords

Public Health Enzyme Activity Internal Medicine Pyruvate Metabolic Disease 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© SSIEM and Kluwer Academic Publishers 1989

Authors and Affiliations

  • A. Kitano
    • 1
  • F. Endo
    • 1
  • Y. Kuroda
    • 2
  • S. Aso
    • 3
  • T. Kawasaki
    • 3
  • I. Matsuda
    • 1
  1. 1.Department of PediatricsKumamoto University Medical SchoolKumamoto
  2. 2.Department of Pediatrics, School of MedicineTokushima UniversityTokushima
  3. 3.Department of PediatricsJapan Red Cross Medical CenterTokyo

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