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Research Article Free access | 10.1172/JCI106986
Mental Retardation Center, University of California, Los Angeles Medical School, Los Angeles, California 90024
National Institute of Arthritis and Metabolic Diseases, the National Heart and Lung Institute, and Clinical Laboratories of the National Institutes of Health, Bethesda, Maryland 20014
Find articles by Blass, J. in: JCI | PubMed | Google Scholar
Mental Retardation Center, University of California, Los Angeles Medical School, Los Angeles, California 90024
National Institute of Arthritis and Metabolic Diseases, the National Heart and Lung Institute, and Clinical Laboratories of the National Institutes of Health, Bethesda, Maryland 20014
Find articles by Schulman, J. in: JCI | PubMed | Google Scholar
Mental Retardation Center, University of California, Los Angeles Medical School, Los Angeles, California 90024
National Institute of Arthritis and Metabolic Diseases, the National Heart and Lung Institute, and Clinical Laboratories of the National Institutes of Health, Bethesda, Maryland 20014
Find articles by Young, D. in: JCI | PubMed | Google Scholar
Mental Retardation Center, University of California, Los Angeles Medical School, Los Angeles, California 90024
National Institute of Arthritis and Metabolic Diseases, the National Heart and Lung Institute, and Clinical Laboratories of the National Institutes of Health, Bethesda, Maryland 20014
Find articles by Hom, E. in: JCI | PubMed | Google Scholar
Published July 1, 1972 - More info
Cultured skin fibroblasts from a 3 yr old girl with severe, diffuse neurologic disease and persistant lactic acidosis, oxidized radioactive citrate, palmitate, and pyruvate at less than one-third the rate of control cells. Her fibroblasts oxidized isocitrate and glutamate at rates comparable with controls. In disrupted cells from this patient, the activity of aconitate hydratase appeared normal. The binding of citrate to aconitate hydratase and the activities of the NAD- and NADP-linked isocitrate dehydrogenases were also normal, while the activity of citrate synthase was slightly below control values. A significant defect was, however, apparent in the activity of the pyruvate dehydrogenase complex although not in the thiamine-dependent first enzyme of that complex. This patient appears to have a partial genetic defect affecting the tricarboxylic acid cycle.