Caracterização parcial dos polipeptídeos de uma fração_ATPase isolada de encéfalo de rata
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 weig...
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| Tipo de recurso: | tesis de maestría |
| Estado: | Versión publicada |
| Fecha de publicación: | 1997 |
| País: | Brasil |
| Institución: | Universidade Federal de Uberlândia (UFU) |
| Repositorio: | Repositório Institucional da UFU |
| Idioma: | portugués |
| OAI Identifier: | oai:repositorio.ufu.br:123456789/27211 |
| Acceso en línea: | https://repositorio.ufu.br/handle/123456789/27211 http://dx.doi.org/10.14393/ufu.di.1997.4 |
| Access Level: | acceso abierto |
| Palabra clave: | Polipeptídeos Cérebro de ratas CNPQ::CIENCIAS BIOLOGICAS::GENETICA |
| Sumario: | 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. |
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