Photobiomodulation increases mitochondrial citrate synthase activity in rats submitted to aerobic training.

This study investigated the effects of photobiomodulation by low-laser laser therapy (LLLT) on the activities of citrate synthase (CS) and lactate dehydrogenase (LDH) and the anaerobic threshold (AT) in rats submitted to treadmill exercise. Fifty-four rats were allocated into four groups: rest control (RCG), rest laser (RLG), exercise control (ECG), and exercise laser (ELG). The infrared LLLT was applied daily on the quadriceps, gluteus maximum, soleus, and tibialis anterior muscles. Muscle samples (soleus, tibialis anterior, and cardiac muscles) were removed 48 h after the last exercise session for spectrophotometric analysis of the CS and LDH. The CS activity (µmol/protein) in ELG (16.02 and 0.49) was significantly greater (P < 0.05) than RCG (2.34 and 0.24), RLG (6.25 and 0.17), and ECG (6.76 and 0.26) in the cardiac and soleus muscles, respectively. The LDH activity (in 1 Mm/protein) in soleus muscle was smaller (P < 0.05) for ELG (0.33) compared to ECG (0.97), RLG (0.79), and RCG (1.07). For cardiac muscle, the LDH activity was smaller (P < 0.05) in ELG (1.38) compared to ECG (1.91) and RCG (2.55). The ECG and ELG showed increases in the maximum speed and a shift of the AT to higher effort levels after the training period, but no differences occurred between the exercised groups. In conclusion, the aerobic treadmill training combined with LLLT promotes an increase of oxidative capacity in this rat model, mainly in muscles with greater aerobic capacity.

Intraerythrocytic organic phosphates and hemoglobins of skua - Catharacta maccormicki (Stercoraridae): at two different stages of the year in relation to Antartic migration

Catharacta maccormicki blood samples were collected in the winter (October) and in the summer (February) in order to study the intraerythrocytic organic phosphates, hemoglobin (Hb) electrophoretic patterns, oxygen blood equilibrium and stripped Hbs, as well as the effect of 2,3-biphosphoglycerate (BPG) and inositol hexaphosphate (IHP) on oxygen affinity. All the samples (five from the winter and five from the summer) showed the same electrophoretic pattern: one minor fast component and one major slow one. No differences in oxygen affinity and Bohr effect in the samples collected in the winter and in the summer were found. Oxygen affinity was higher in the stripped Hb than in the blood. BPG seemed to have no effect on the functional properties of skua Hb while IHP does. No BPG was found in any sample. Both inositol pentaphosphate (IP5) and IHP were found in all the samples. The IP5/IHP ratio in the winter samples was 3.0 while in summer 3.5. Adenosine diphosphate (ADP) was found in samples from both the seasons. Adenosine monophosphate (AMP) and adenosine triphosphate (ATP) were present only in the summer samples while guanosine triphosphate (GTP) was found in the winter samples. Since IP5 and IHP are very powerful HB allosteric effectors, ATP and GTP might function as other protein modulators.

Soluble malate dehydrogenase of Geophagus brasiliensis (Cichlidae, Perciformes): isolated isoforms and kinetics properties

Kinetic properties and thermal stabilities of Geophagus brasiliensis skeletal muscle unfractionated malate dehydrogenase (MDH, EC 1.1.1.37) and its isolated isoforms were analyzed to examine a possible sMDH-B* locus duplication in a fixation process influenced by genetic drift. Two optimal pHs were detected: 7.5 for AB1 unfractionated muscle phenotype and its B1 isoform, and 8.0 for AB1B2 unfractionated muscle phenotype, A and B2 isoforms. While G. brasiliensis A isoform could be characterized as thermostable, the duplicated B isoform cannot be assumed as thermolabile. Km values for isolated B2 isoforms were 1.6 times lower than for B1. A duplication event in progress best explains the electrophoretic six-band pattern detected in G. brasiliensis, which would be caused by genetic drift.