Increased lactate threshold after five weeks of treadmill aerobic training in rats.

The aim of the present study was to analyse the lactate threshold (LT) changes in rats submitted to an aerobic treadmill-training programme. Twenty-five Wistar rats were divided into two groups: a sedentary control group (CG), and a trained group (TG) submitted to an aerobic training during 5 weeks. All the animals were submitted to an incremental treadmill exercise test in order to determine LT. There was an increase in the maximum running speed in the TG (from 32.25 ± 1.27 to 47.75 ± 3.13 m.min-1 - p = 0.001), and running speed at LT (from 26.21 ± 1.15 to 35.30 ± 2.24 m.min-1 - p = 0.004), a part from the reduction in blood lactate at LT. LT can be determined in rats, and aerobic training induced positive oxidative physiological adaptations in the animals.

Adaptação enzimática da LDH em ratos submetidos a treinamento aeróbio em esteira e laser de baixa intensidade / Adaptation of LDH enzyme in rats undergoing aerobic treadmill training and low intensity laser therapy

OBJETIVO: Verificar a atividade e padrão eletroforético da LDH em resposta ao exercício em esteira em ratos submetidos à fotoestimulação por laser de baixa intensidade (780 etam). MÉTODO: Foram utilizados nesse estudo 54 ratos machos jovens (30dias), Winstar, com peso inicial médio de 112 ± 4,7g, os quais foram divididos em quatro grupos: dois permaneceram em repouso, GRC (grupo repouso controle, n= 9) e GRL (grupo repouso laser, n= 10), sendo o segundo irradiado por laser, e outros dois foram submetidos ao treinamento aeróbio e testes de esforço crescente em esteira (em degraus descontínuos) visando à determinação do limiar de anaerobiose (LA) durante 5 semanas, GEC (grupo exercício controle, n= 16) e GEL (grupo exercício laser, n= 19), sendo o último também irradiado por laser. O laser foi aplicado no quadríceps, glúteo máximo, sóleo e tibial anterior (TA), bilateralmente, imediatamente após cada sessão de treinamento, usando: 3,8J/cm², 15mW, 10s, modo contínuo, durante 5 semanas. Amostras de sóleo, TA e coração foram removidas 48 horas após a última sessão de exercício para análise eletroforética e espectrofotométrica. A estatística foi realizada através do teste ANOVA e post-hoc de TUKEY. O nível de significância foi considerado (p< 0,05). RESULTADOS: Foram observadas reduções na atividade da LDH causadas pelo laser (de 19 por cento a 30 por cento), exercício (de 41 por cento a 66 por cento) e as ações combinadas (de 47 por cento a 66 por cento) (p< 0,01). A eletroforese mostrou uma predominância da subunidade B para o sóleo e coração, e uma predominância da subunidade A no TA. CONCLUSÕES: Estes dados sugerem uma melhor resposta adaptativa dos animais ao treinamento aeróbio associado à terapia laser, no que se refere à otimização da via oxidativa.

Isoform expression in the multiple soluble malate dehydrogenase of Hoplias malabaricus (Erythrinidae, Characiformes)

Kinetic properties and thermal stabilities of Hoplias malabaricus liver and skeletal muscle unfractionated malate dehydrogenase (MDH, EC 1.1.1.37) and its isolated isoforms were analyzed to further study the possible sMDH-A* locus duplication evolved from a recent tandem duplication. Both A (A1 and A2) and B isoforms had similar optima pH (7.5-8.0). While Hoplias A isoform could not be characterized as thermostable, B could as thermolabile. A isoforms differed from B isoform in having higher Km values for oxaloacetate. The possibly duplicated A2 isoform showed higher substrate affinity than the A1. Hoplias duplicated A isoforms may influence the direction of carbon flow between glycolisis and gluconeogenesis

Astyanax scabripinnis (Pisces: Characidae) hemoglobins: structure and function

Electrophoretic patterns of hemoglobins, Root effect, Bohr effect in blood and stripped hemoglobin, Hb-O2 affinity GTP modulation of Astyanax scabripinnis (lambari), caught at three different altitudes in Ribeiräo Grande, near Campos do Jordäo (Säo Paulo), are described. All populations showed the same electrophoretic patterns: two cathodal components in starch gel. Normal Bohr effect values were found in these three populations both in blood (phi = -0,11) and stripped hemoglobin (phi = -0,12). Different blood O2 affinities collected in fish of these 3 populations were detected. GTP has a large influence on Hb-O2 binding properties in A. scabripinnis. Stripped hemoglobin shows small Root effect. The addition of triphosphated nucleotides increases this effect. GTP is more effective than ATP on enhancing Root effect. Oxygen availability in water can be the factor responsible for differences found in blood O2 affinity

Functional properties of the three hemoglobin phenotypes of Nelore cattle

Blood and stripped hemoglobin from Nelore cattle individuals were submitted to oxygen equilibrium experiments in both gasometric and spectrophotometric methods. No difference was detected in oxygen affinity and Bohr effect among Hb A, Hb B and Hb AB in experiments with both blood and stripped hemoglobin, in the presence and absence of the chloride ion. However, n values (Hill plots) were higher in Hb B and Hb AB (>2) than in Hb A (<2)

Astyanax scabripinnis (Pisces: Characidae) hemoglobins: structure and function.

Electrophoretic patterns of hemoglobins, Root effect, Bohr effect in blood and stripped hemoglobin, Hb-O2 affinity GTP modulation of Astyanax scabripinnis (lambari), caught at three different altitudes in Ribeirão Grande, near Campos do Jordão (São Paulo), are described. All populations showed the same electrophoretic patterns: two cathodal components in starch gel. Normal Bohr effect values were found in these three populations both in blood (phi = -0.11) and stripped hemoglobin (phi = -0.12). Different blood O2 affinities collected in fish of these 3 populations were detected. GTP has a large influence on Hb-O2 binding properties in A. scabripinnis. Stripped hemoglobin shows small Root effect. The addition of triphosphated nucleotides increases this effect. GTP is more effective than ATP on enhancing Root effect. Oxygen availability in water can be the factor responsible for differences found in blood O2 affinity.