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Biochemical nature of pyruvate dehydrogenase complex in the patient with primary lactic acidaemia
Author(s) -
Kitano A.,
Endo F.,
Kuroda Y.,
Aso S.,
Kawasaki T.,
Matsuda I.
Publication year - 1989
Publication title -
journal of inherited metabolic disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 102
eISSN - 1573-2665
pISSN - 0141-8955
DOI - 10.1007/bf01802031
Subject(s) - pyruvate dehydrogenase complex , protein subunit , enzyme , biochemistry , pyruvate dehydrogenase kinase , dihydrolipoyl transacetylase , pyruvate dehydrogenase phosphatase , branched chain alpha keto acid dehydrogenase complex , pyruvate decarboxylation , oxoglutarate dehydrogenase complex , pyruvate kinase , biology , chemistry , dehydrogenase , glycolysis , gene
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 apparent K m value of the enzyme was similar to the control value. The immunoblot pattern of each subunit protein, E 1α , E 1β , the component X, E 2 and E 3 , 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.