Abstract
A specific diaphorase was defective in cultured skin fibroblasts from a patient with Luft disease (giant mitochondrial disease; nonthyroid hypermetabolism). In homogenates of whole cells, diaphorase activity was 124±8 nmol/min/mg protein, compared to 425±40 in 14 controls. On fractionation of the cells with digitonin, the whole decrease was attributable to a decrease in the soluble fraction (57±11 vs 597±73 nmol/min/mg protein). The decrease persisted with NADPH as substrate as well as NADH, and with several electron acceptors. On electrophoresis and activity staining, the Luft cells lacked the major, cathodic, FAD-dependent protein with diaphorase activity. The pathophysiological significance of the deficiency of this diaphorase has not been studied, but the defect might impair the regulation of metabolism by altering the control of cellular redox state.
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Piacentini-Sorbi, S., Sheu, KF.R. & Blass, J.P. Deficiency of a specific diaphorase in Luft disease fibroblasts. Neurochemical Pathology 1, 147–157 (1983). https://doi.org/10.1007/BF02834195
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DOI: https://doi.org/10.1007/BF02834195