Caracterização parcial dos polipeptídeos de uma fração_ATPase isolada de encéfalo de rata

• Ano de defesa: 1997
• Autor(a) principal: Freitas, Paula Mendes de
• 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: Polipeptídeos; Cérebro de ratas; CNPQ::CIENCIAS BIOLOGICAS::GENETICA
• Link de acesso: https://repositorio.ufu.br/handle/123456789/27211; http://dx.doi.org/10.14393/ufu.di.1997.4

This work consists in the characterization of polypeptides from a fraction enriched in M ​​^ -ATPasic activity obtained from supernatant 38,900 g of rat brain using phosphocellulose column (Santos, 1997). In this fraction a myosin II heavy chain primed polypeptide is observed, a major molecular weight above several polypeptides between 45-66 kDa. The polypeptide above this is vario ... Main polypeptide cosedimented with actin at 12,000 g in the absence and ATP. The calpain proteolysis assay showed the degradation and .. "4S trrta and high molecular weight polypeptides, polypeptides between 66-45 KDa and to ppp with the onset of approximately 13 KD. besides others along with bromophenol. The main polypeptide and the 130 kDa fraction were labeled by specific subunit specific antibody given the main polypeptide was that of fodrin. Corroborating this data, P P p is retained on the CaM-Agarose column. tU Tmm npoolliippeepptideo above CaM-Agarose fodra 1 «a. The 50 KDa polypeptide was also retained on the column. . Phosphocellulose, and was proteolyzed by calpain and retained as shown by immunoblotting the α-subunit of CaM-kinases, endogenous phosphorylation. Inactivating the protein became inactive, losing it during preparation and in the ability to autophosphorylate and to phosphorylate other polypeptides from the PC fraction.