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Long-Chain Acyl-Coenzyme A Dehydrogenase Deficiency: Biochemical Studies in Fibroblasts from Three Patients
Journal article   Open access   Peer reviewed

Long-Chain Acyl-Coenzyme A Dehydrogenase Deficiency: Biochemical Studies in Fibroblasts from Three Patients

Brad A Amendt, Ann Moon, Lisa Teel and William J Rhead
Pediatric research, Vol.23(6), pp.603-605
06/1988
DOI: 10.1203/00006450-198806000-00015
PMID: 3393393
url
https://doi.org/10.1203/00006450-198806000-00015View
Published (Version of record) Open Access

Abstract

We studied fibroblasts from three patients with long-chain acyl-coenzyme A dehydrogenase (LCADH) deficiency; siblings H.C. and J.C. had milder clinical phenotypes than unrelated patient R-l. In H.C, J.C, and R-l oxidation of [9,10(n)-3H]palmitate was 50, 48, and 28% of control, respectively, with R-l having significantly less activity than H.C. and J.C. (p < 0.05). Assays of mitochondrial shortchain and medium-chain acyl-coenzyme A dehydrogenases were normal in H.C. and J.C. However, mitochondrial LCADH activities in all three ranged from 17 to 21% of control. Flavin adenine dinucle-otide addition increased LCADH activities in all three to 27-36% of control. In the presence of monospecific mediumchain acyl-coenzyme A dehydrogenase antiseria, LCADH activity decreased 17% in controls, and fell to <11% of control in J.C. and R-l. The heterogeneity observed in the [3H]palmitate oxidation studies was not ex­plained by differences in LCADH activities under any assay condition. © 1988 International Pediatrics Research Foundation, Inc.

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