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Lacticacidaemia due to pyruvate dehydrogenase deficiency, with evidence of protein polymorphism in the α-subunit of the enzyme

By Jess G. Thoene, R. Petrova-Benedict, N. McKay, W. Wilson, B. Robinson and B. Bergen


In three infants with neonatal lacticacidaemia, a deficiency in the E 1 (pyruvate dehydrogenase) component of the pyruvate dehydrogenase complex was demonstrated in skin fibroblast cultures. Residual activites of the pyruvate dehydrogenase complex in the activated state were 1.6%, 3.9% and 18.8% of control values, respectively. Immunoprecipitation of extracts of cultures skin fibroblasts grown on 35 S-methionine with anti-pyruvate dehydrogenase complex antibody revealed an abnormality in the E 1 α-component of these three patients when visualised after sodium dodecyl sulphate/polyacrylamide gel electrophoresis. This component appeared to have a slightly lower molecular weight than did this protein from control cell strains. Cell strains from other patients with a deficiency of the pyruvate dehydrogenase complex did not exhibit this defect. Three patients also showed dysmorphism and developmental abnormalities of the central nervous system

Publisher: Springer-Verlag
Year: 1986
DOI identifier: 10.1007/BF00441736
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