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Research Article Free access | 10.1172/JCI106110
Department of Pediatrics, New York University School of Medicine, New York 10016
Department of Medicine, New York University School of Medicine, New York 10016
Department of Pediatrics, Tulane Medical School, New Orleans, Louisiana 70112
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Department of Pediatrics, New York University School of Medicine, New York 10016
Department of Medicine, New York University School of Medicine, New York 10016
Department of Pediatrics, Tulane Medical School, New Orleans, Louisiana 70112
Find articles by Hutzler, J. in: JCI | PubMed | Google Scholar
Department of Pediatrics, New York University School of Medicine, New York 10016
Department of Medicine, New York University School of Medicine, New York 10016
Department of Pediatrics, Tulane Medical School, New Orleans, Louisiana 70112
Find articles by Cox, R. in: JCI | PubMed | Google Scholar
Department of Pediatrics, New York University School of Medicine, New York 10016
Department of Medicine, New York University School of Medicine, New York 10016
Department of Pediatrics, Tulane Medical School, New Orleans, Louisiana 70112
Find articles by Woody, N. in: JCI | PubMed | Google Scholar
Published August 1, 1969 - More info
Fibroblasts grown in tissue culture from the skin of normal subjects have lysine-ketoglutarate reductase activity (lysine: α-ketoglutarate: triphosphopyridine nucleotide (TPNH) oxidoreductase (ε-N-[L-glutaryl-2]-L-lysine forming)). The activity of the enzyme is considerably reduced in the skin fibroblasts grown from three siblings with hyperlysinemia. The high concentrations of lysine in the blood of these patients, the previous demonstration in the intact subject of a reduction in the ability to degrade lysine, and the present demonstration of diminished lysine-ketoglutarate reductase activity, accurately define the metabolic defect and establish the saccharopine (ε-N-[L-glutaryl-2]-L-lysine) pathway as the major degradative pathway for lysine in the human.