Gross efficiency and energy expenditure in kayak ergometer exercise.

We purposed to study energy expenditure, power output and gross efficiency during kayak ergometer exercise in 12 elite sprint kayakers. 6 males (age 24.2±4.8 years, height 180.4±4.8 cm, body mass 79.7±8.5 kg) and 6 females (age 24.3±4.5 years, height 164.5±3.9 cm, body mass 65.4±3.5 kg), performed an incremental intermittent protocol on kayak ergometer with VO2 and blood lactate concentration assessment, a non-linear increase between power output and energy expenditure being observed. Paddling power output, energy expenditure and gross efficiency corresponding to VO2max averaged 199.92±50.41 W, 75.27±6.30 ml.kg - 1.min - 1, and 10.10±1.08%. Male kayakers presented higher VO2max, power output and gross efficiency at the VO2max, and lower heart rate and maximal lactate concentration than females, but no differences were found between genders regarding energy expenditure at VO2max. Aerobic and anaerobic components of energy expenditure evidenced a significant contribution of anaerobic energy sources in sprint kayak performance. Results also suggested the dependence of the gross efficiency on the changes in the amount of the aerobic and anaerobic contributions, at heavy and severe intensities. The inter-individual variance of the relationship between energy expenditure and the corresponding paddling power output revealed a relevant tracking for females (FDγ=0.73±0.06), conversely to the male group (FDγ=0.27±0.08), supporting that some male kayakers are more skilled in some paddling intensities than others.

Metabolic evaluation of cooled equine spermatozoa.

Microscopy has been used in the routine evaluation of sperm metabolism. Nevertheless, it has limited capacity to preview male fertility. As calorimetry may be used to evaluate directly the metabolic activity of a biological system, the aim of this study was to use microcalorimetry as an additive method for sperm metabolism evaluation of cooled equine semen. Two ejaculates of four stallions were collected and motility, viability (eosin 3%) and membrane functional integrity (hyposmotic swelling test) of spermatozoa were evaluated. Sperm samples were processed following different protocols and the metabolism of these samples was accessed by calorimetry. Centrifugation is part of some of these processing protocols and although this procedure has been deleterious for sperm viability and plasma membrane integrity, no decrease in sperm motility was observed. Microcalorimetry was capable of detecting the positive effect of re-suspending the sperm pellet with Kenney extender. Thus, the use of microcalorimetry offered additional information for equine sperm metabolism evaluation and was efficient in detecting important information from sperm cell metabolism.

A novel and efficient and low-cost methodology for purification of Macrotyloma axillare (Leguminosae) seed lectin.

The N-acetyl-galactosamine specific lectin from Macrotyloma axillare seeds (LMA) was purified by precipitation and ion exchange chromatography. The LMA 0.2 mol L(-1) fraction showed hemagglutinating activity on erythrocytes A1. The results for molecular mass determinations were about 28 kDa. The LMA pH-dependent assays showed best hemagglutinating activity at pH 6.0-8.0; being decreased at acidic/alkaline conditions and by EDTA treatment. LMA is a tetramer at pH 8.2 and a dimer at pH 4.0. Human erythrocytes from ABO system confirmed the A1 specificity for LMA. This new methodology is useful and easy, with low costs, for lectin purification in large amounts.

Physical-chemical characterization and stability study of alpha-trypsin at pH 3.0 by differential scanning calorimetry.

alpha-Trypsin is a serine-protease with a polypeptide chain of 223 amino acid residues and six disulfide bridges. It is a globular protein with predominance of antiparallel ss-sheet secondary structure and it has two domains with similar structures. In the present work, a stability study of alpha-trypsin in the acid pH range was performed and some physical-chemical denaturation parameters were measured by using differential scanning calorimetry (DSC). The alpha-trypsin has a shelf-life (t(95%)) of about 10 months at pH 3.0 and 4 degrees C and its hydrolysis into the psi-trypsin isoform is negligible during 6 months. The observed ratio DeltaH(cal)/DeltaH(vH) is close to unity, which suggests the occurrence of a two-state transition. At pH 3.0, alpha-trypsin unfolded with T(m) = 325.9 K and DeltaH = 99.10 kcal mol(-1), and the change in heat capacity between the native and unfolded forms of the protein was estimated to be 1.96+/-0.18 kcal mol(-1)K(-1). The stability of alpha-trypsin calculated at 298 K was DeltaG(U)=6.10 kcal mol(-1) at pH 3.0. These values are in the range expected for a small globular protein. These results show that the thermodynamic parameters of unfolding of beta-trypsin do not change substantially after its conversion to alpha-trypsin.

Characterization of -trypsin at acid pH by differential scanning calorimetry.

Trypsin is a serino-protease with a polypeptide chain of 223 amino acid residues and contains six disulfide bridges. It is a globular protein with a predominance of antiparallel -sheet and helix in its secondary structure and has two domains with similar structures. We assessed the stability of -trypsin in the acid pH range using microcalorimetric (differential scanning calorimetry) techniques. Protein concentrations varied in the range of 0.05 to 2.30 mg/ml. Buffer solutions of 50.0 mM -alanine and 20.0 mM CaCl2 at different pH values (from 2.0 to 4.2) and concentrations of sorbitol (1.0 and 2.0 M), urea (0.5 M) or guanidinium hydrochloride (0.5 and 1.0 M) were used. The data suggest that we are studying the same conformational transition of the protein in all experimental situations using pH, sorbitol, urea and guanidinium hydrochloride as perturbing agents. The observed van't Hoff ratios (deltaHcal/deltaHvH) of 1.0 to 0.5 in the pH range of 3.2 to 4.2 suggest protein aggregation. In contrast, deltaHcal/deltaHvH ratios equal to one in the pH range of 2.0 to 3.2 suggest that the protein unfolds as a monomer. At pH 3.00, -trypsin unfolded with Tm = 54 C and deltaH = 101.8 kcal/mol, and the change in heat capacity between the native and unfolded forms of the protein (deltaCp) was estimated to be 2.50 0.07 kcal mol-1 K-1. The stability of -trypsin calculated at 298 K was deltaG D = 5.7 kcal/mol at pH 3.00 and deltaG D = 15.2 kcal/mol at pH 7.00, values in the range expected for a small globular protein.

Characterization of á-trypsin at acid pH by differential scanning calorimetry

Trypsin is a serino-protease with a polypeptide chain of 223 amino acid residues and contains six disulfide bridges. It is a globular protein with a predominance of antiparallel á-sheet and helix in its secondary structure and has two domains with similar structures. We assessed the stability of á-trypsin in the acid pH range using microcalorimetric (differential scanning calorimetry) techniques. Protein concentrations varied in the range of 0.05 to 2.30 mg/ml. Buffer solutions of 50.0 mM á-alanine and 20.0 mM CaCl2 at different pH values (from 2.0 to 4.2) and concentrations of sorbitol (1.0 and 2.0 M), urea (0.5 M) or guanidinium hydrochloride (0.5 and 1.0 M) were used. The data suggest that we are studying the same conformational transition of the protein in all experimental situations using pH, sorbitol, urea and guanidinium hydrochloride as perturbing agents. The observed van't Hoff ratios (deltaHcal/deltaHvH) of 1.0 to 0.5 in the pH range of 3.2 to 4.2 suggest protein aggregation. In contrast, deltaHcal/deltaHvH ratios equal to one in the pH range of 2.0 to 3.2 suggest that the protein unfolds as a monomer. At pH 3.00, á-trypsin unfolded with Tm = 54ºC and deltaH = 101.8 kcal/mol, and the change in heat capacity between the native and unfolded forms of the protein (deltaCp) was estimated to be 2.50 ± 0.07 kcal mol-1 K-1. The stability of á-trypsin calculated at 298 K was deltaG D = 5.7 kcal/mol at pH 3.00 and deltaG D = 15.2 kcal/mol at pH 7.00, values in the range expected for a small globular protein.

Prevalência de dor osteomuscular na equipe de enfermagem do Hospital da Polícia Militar de Minas Gerais / Prevalence of Osteomuscular pain in the nursing staff of the Militar Policy Hospital of Minas Gerais

O registro de distúrbios osteomusculares tem se tornado mais frequente entre a população trabalhadora, incluindo, neste grupo, os profissionais de enfermagem. O objetivo deste estudo foi identificar a prevalência de dor osteomuscular na equipe de enfermagem do Hospital da Polícia Militar de Minas Gerais (HPM-MG) e sua associação com características relacionadas ao trabalho. Estudo transversal, onde a versão brasileira do Questionário Nórdico foi aplicada a uma amostra de 167 auxiliares e técnicos de enfermagem do HPM. Foi elaborado um protocolo para a caraccterização dos participantes contendo variáveis sociodemográficas e ocupacionais e perguntas sobre atividades relacionadas com o trabalho. Teste t de Student e Qui-quadrado foram utilizados para a análise dos dados. Entre os 167 entrevistados, 110 (65 por cento)eram mulheres e 160 (96 por cento) relataram sentir dor pelo menos em uma região do corpo. A região mais frequente afetada pela dor foi a coluna lombar (70 por cento). Houve associação entre a presença de dor osteomuscular e o turno de trabalho, realização de tarefas repetitivas, trabalhar na posição encurvada, levantar ou transferir pacientes, empurrar objetos pesados, não adotar medidas preventivas como alongamentos e exercícios, não realizar atividade física regular ou atividade de lazer (p,0,05). Os resultados mostraram que muitas atividades realizadas durante o trabalho estão relacionadas à presença de sintomas osteomusculares. A fisioterapia pode ser uma possibilidade real de intervenção com, adoção de medidas educativas e preventivas no ambiente de trabalho. São necessários estudos que investiguem a eficácia das técnicas preventivas no tratamento dos sintomas osteomusculares relacionados ao trabalho