Palmitate oxidation and some enzymes of energy metabolism in human muscles and cultured muscle cells.

1. Palmitate oxidation rates and activities of creatine kinase, cytochrome c oxidase and citrate synthase were determined in homogenates of three different human muscles and their derived muscle cell cultures. Palmitate oxidation was also assayed in intact cultured cells (myotubes). 2. Biopsies obtained from m. rectus abdominis exhibited a lower palmitate oxidation rate and lower activities of citrate synthase and cytochrome c oxidase than those from m. gluteus and m. quadriceps. In contrast, cell cultures obtained from the three muscles were mutually comparable with regard to these mitochondrial activities. 3. Although cell cultures only reached a low differentiation grade (judged by the total creatine kinase activity and percentage isoenzyme-MM) they are well comparable with the original biopsies with respect to citrate synthase activity and capacity of palmitate oxidation. The activity of cytochrome c oxidase was clearly lower in the cultured cells. 4. Palmitate was more completely oxidized in intact myotubes than in homogenates of myotubes. Apparent Km and Vmax values of palmitate oxidation did not differ significantly in homogenates and intact preparations of myotubes.