Caracterização parcial de uma ATPase de citosol de encéfalo de rato

• Ano de defesa: 2001
• Autor(a) principal: Pinheiro, Carla Mônica
• Tipo de documento: Dissertação
• Tipo de acesso: Acesso aberto
• Idioma: por
• Instituição de defesa: Universidade Federal de Uberlândia; Brasil; Programa de Pós-graduação em Genética e Bioquímica
• Palavras-chave em Português: Proteínas; Adenosinatrifosfatase; Purificação; Inibidores enzimáticos; CNPQ::CIENCIAS BIOLOGICAS::GENETICA
• Link de acesso: https://repositorio.ufu.br/handle/123456789/27209; http://dx.doi.org/10.14393/ufu.di.2001.15

This work presents the obtention of rich ATPase-activity fraction from rat encephalon cytosol. The encephalon homogenized was centrifuged 50.000 x g for 40 minutes and the supernatant Ioaded in SP-Sepharose column. The flow through was treated with ammoníum sulfate and Ioaded. i■n Q-Seoenphhaarroossee column. Its flow through was treated with 30 % ammonium sulfat.eo aanndd ATPase activity was resíored by centrifugation. This fraction showed, MMgn2+-ATPase activity, however, the Ca2+-ATPase activity was zero. N.. o K^/ P/ OTA-ATPase activity was detecíed. The Mg2+- ATPase activity was hu-i flher tfhhaann GuTirPaase activity. Alumminium fluoride inhibited about 3„0„ o/o, AATTPase activity. Azide and vanadate had no effective activity; 0,2 % Triton Xv- 4nn and high salt concentraíion inhibited about 60 % activity. The ScnDqo PAGE analysis showed two evident 160 and 5455 polypeptides. Thís probable ATPase doesrft interact with ionic exchange columns and its activity showed different properties of know ATPases such as Ca2+-ATPase, FiF0-ATPase, Na+/K+-ATPase, myosins, kinesin and dynein.