| Abstract: | Enzymes of fatty acid activation and transport were studied in luteinized rat ovaries. Luteal mitochondria were found to contain high levels of palmitoyl-CoA synthetase and carnitine palmitoyl-transferase activities. In addition, studies on the effect of palmitate concentration on palmitoyl-CoA synthetase activity revealed the possible existence of two forms of the enzyme: Km values of 0.34 mM and 21.33 mM, with Vmax of 3.64 and 66.67 nmoles/min/mg mitochondrial protein respectively, were obtained for the two activities. Similar kinetic data for carnitine palmitoyl-transferase activity in intact mitochondria are a Km of 21 microM and a Vmax of 18.2 nmoles/min/mg mitochondrial protein. Only one activity of this enzyme could be detected in luteal mitochondria. It appears that the activities of both enzymes were not affected by prior administration of LH in vivo. The possibility that this negative finding was due to the experimental procedures employed, rather than a reflection of the situation in vivo, could not be discounted, although its more likely that these two enzymes are probably not locus of LH stimulation. The results indicate that fatty acid oxidation is an important metabolic capability of luteal mitochondria, and support the view regarding the lipid nature of the respiratory fuel of ovarian tissue. |
