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Beta‐oxidation enzymes in normal human muscle and in muscle from a patient with an unusual form of myopathic carnitine deficiency
Author(s) -
Trevisan Carlo P.,
Reichmann Heinz,
DeVivo Darryl C.,
DiMauro Salvatore
Publication year - 1985
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880080809
Subject(s) - carnitine , muscle biopsy , mitochondrial myopathy , beta oxidation , endocrinology , myopathy , medicine , coenzyme a , dehydrogenase , acyl coa dehydrogenase , enzyme , flavoprotein , mitochondrion , biology , muscle tissue , biopsy , biochemistry , metabolism , mitochondrial dna , gene , reductase
In a reported patient with myopathic carnitine deficiency, addition of exogenous carnitine to muscle homogenates failed to correct palmitate oxidation, and oral carnitine was of no clinical benefit. 27 In a muscle biopsy from this patient, we found that, in contrast to the marked deficiency of free carnitine (3% of normal) short‐ and medium‐chain acylcarnitines were in the normal range and long‐chain acylcarnitine was increased almost four times. As this result confirmed the hypothesis of a muscle defect of mitochondrial oxidation of palmitate, all eight enzymes of beta‐oxidation were measured spectrophotometrically in the muscle extract. None of them was found to be defective. These data suggest that the underlying biochemical abnormality in this patient may be a deficiency of the carnitine–acylcarnitine translocase system or a defective interaction between acyl‐CoA dehydrogenase and its flavoprotein coenzyme.