Skeletal muscle fatigue in long-distance runners, sprinters and untrained men after repeated drop jumps performed at maximal intensity.

One hundred drop jumps were performed at maximal intensity every 20 s in 12 untrained subjects (UT), 9 sprinters (S) and 10 long-distance runners (LDR). Muscle contraction force (P20, P50) induced by percutaneous electrical stimulation (20 Hz and 50 Hz, respectively) as well as maximal voluntary contraction force and the height of vertical jumps performed in different ways decreased (P<0.05) and was not restored to the initial value 20 min post exercise.

Tetraphenylphosphonium inhibits oxidation of physiological substrates in heart mitochondria.

We show that tetraphenylphosphonium inhibits oxidation of palmitoylcarnitine, pyruvate, malate, 2-oxoglutarate and glutamate in heart mitochondria in the range of concentration (1-5 microM) commonly used for the determination of mitochondrial membrane potential. The inhibition of 2-oxoglutarate (but not other substrate) oxidation by tetraphenylphosphonium is dependent on the concentration of 2-oxoglutarate and on extramitochondrial free calcium, and the kinetic plots are consistent with a mixed type of inhibition. Our results indicate that tetraphenylphosphonium interacts with enzymes, specifically involved in the oxidation of 2-oxoglutarate, most possibly, 2-oxoglutarate dehydrogenase.

[Functional changes in the mitochondrial site of adenylate kinase and creatine kinase systems of energy transport induced by myocardial ischemia and adriablastin].

Under effects of myocardial ischemia (30 min), the activities of the intermembrane enzymes of rabbit heart mitochondria, i.e., adenylate kinase and creatine kinase, are inhibited by 20% and 23%, respectively.

[The role of adenylate kinase in the regulation of the rate and effectiveness of energy transfer from mitochondria to hexokinase in vitro].

The effect of adenylate kinase activity on the rate and efficiency of energy transport from mitochondria to hexokinase was studied in a system containing isolated rabbit heart mitochondria, hexokinase and adenylate kinase at low concentrations of adenine nucleotides. Oxygen consumption by mitochondria and glucose-6-phosphate synthesis by hexokinase were recorded. It was found that with adenylate kinase being active both in mitochondria and in the washing solution, the rate and efficiency of glucose-6-phosphate synthesis considerably increases.

The effect of adenylate kinase activity on the rate and efficiency of energy transport from mitochondria to hexokinase.

The rate and efficiency of energy transport were examined in a system containing isolated rabbit heart mitochondria, hexokinase, adenylate kinase and low concentrations of adenine nucleotides. Oxygen consumption by mitochondria and glucose-6-phosphate synthesis by hexokinase were registered. It was found that when adenylate kinase is active both in mitochondria and in the environmental solution, the rate and efficiency (glucose-6-phosphate/O ratio) of glucose-6-phosphate formation considerably increase.