RESUMO
Chagas disease (CD) is a parasitic infection that originated in the Americas and is caused by Trypanosoma cruzi. In the last few years, the disease has spread to countries in North America, Asia and Europe due to the migration of Latin Americans. In the Brazilian Amazon, CD has an endemic transmission, especially in the Rio Negro region, where an occupational hazard was described for piaçaveiros (piassaba gatherers). In the State of Amazonas, the first chagasic infection was reported in 1977, and the first acute CD case was recorded in 1980. After initiatives to integrate acute CD diagnostics with the malaria laboratories network, reports of acute CD cases have increased. Most of these cases are associated with oral transmission by the consumption of contaminated food. Chronic cases have also been diagnosed, mostly in the indeterminate form. These cases were detected by serological surveys in cardiologic outpatient clinics and during blood donor screening. Considering that the control mechanisms adopted in Brazil's classic transmission areas are not fully applicable in the Amazon, it is important to understand the disease behavior in this region, both in the acute and chronic cases. Therefore, the pursuit of control measures for the Amazon region should be a priority given that CD represents a challenge to preserving the way of life of the Amazon's inhabitants.
Assuntos
Animais , Digestão/genética , Cavalos/genética , alfa-Amilases Pancreáticas/genética , alfa-Amilases Salivares/genética , Substituição de Aminoácidos , Sequência de Bases , Biodiversidade , Grão Comestível/química , Carboidratos da Dieta , Variação Genética , Técnicas de Genotipagem , Cavalos/classificação , Itália , Polimorfismo de Nucleotídeo Único , Alinhamento de Sequência , Análise de Sequência de DNARESUMO
Alpha-amylase inhibitor extracted from different sources, i.e., wheat grains [Sohag 2 and Giza 164], legume seeds such as cow pea [Carim 7 and Giza 3], and kidney bean [Giza 6 and Giza 133] was purified and tested for activity using human salivary and pancreatic alpha-amylase. Results showed that the alpha-amylase inhibitor activity from samples studied were 120 to 285 unit / mg protein. The inhibitor was found to be stable at pH range from 2 to 4. It was also stable to digestion by proteolytic enzymes [pepsin and trypsin]. The inhibition was faster at 37°C than at 25°C, The results showed that the degree of thermal stability of alpha-amylase inhibitor extracted from kidney bean [Giza 133] was at 35-37°C, activity was decreased on 50°C for 5 hr. Increased of pre-incubation time between inhibitor and both alpha-amylase enzymes at 37°C increased the rate of inhibition of these enzymes and the complex formation between them from 60 - 80% in 30 min, while addition of these enzymes to the mixture containing inhibitor and substrate [without pre-incubation] decrease the percent inhibition. Therefore, an evidence of specific interference of the alpha-amylase inhibitor with starch availability was established. Such possibilities will have valuable interest in the field of special dietary food preparations for diabetes and over weight reduction purposes