Table 1. .
Functional and Enzymatic Investigations of Muscle Tissue[Note]
| Biochemical Measurements | Patient 1 | Controls |
| Substrate oxidation rate (nmol/h/mg protein): | ||
| [1–14C]pyruvate+malate+ADP | 45 | 263–900 |
| [1–14C]pyruvate+carnitine+ADP | 98 | 302–856 |
| [1–14C]pyruvate+malate (−ADP) | 35 | 32–102 |
| [U-14C]malate+pyruvate+malonate+ADP | 37 | 282–874 |
| [U-14C]malate+acetylcarnitine+malonate+ADP | 73 | 273–678 |
| [U-14C]malate+acetylcarnitine+arsenite+ADP | 52 | 156–378 |
| [1,4–14C]succinate+acetylcarnitine+ADP | 24 | 167–488 |
| [1–14C]pyruvate+malate+CCCP | 383 | 304–889 |
| [1–14C]pyruvate+malate+atractylate+ADP | 41 | 115–273 |
| Enzyme activity (unit/g protein): | ||
| Citrate synthase | 196 | 150–325 |
| Complex I | 63 | 28–76 |
| Complex I+III | 136 | 64–218 |
| Complex II | 80 | 39–102 |
| Complex II+III | 108 | 93–180 |
| Complex III | 622 | 426–762 |
| Cytochrome c oxidase | 539 | 452–889 |
| Oligomycin-sensitive ATPase (complex V) | 137 | 70–397 |
| Pyruvate dehydrogenase | 7.2 | 6.1–19.8 |
Note.— Postnuclear supernatant prepared from native, unfrozen muscle showed reduced activities in all ADP-stimulated oxidation reactions but was normal in the presence of the uncoupler CCCP. Analysis of respiratory-chain enzymes, ATPase, and pyruvate dehydrogenase revealed normal activities.