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	Provedor de dados BJMBR (1) Autor Delmar,M. (1) Ek-Vitorin,J.F. (1) Rush,P. (1) Taffet,S.M. (1) Yahuaca,P. (1) Palavra-chave Connexin (1) Phosphorylation (1) Phosphotransferases (1) Protein kinase (1) Tipo do documento Info:eu-repo/semantics/article (1) Ano 2000 (1) País Brazil (1) Idioma Inglês (1)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 1 Primeira ... 1 ... Última Identification of a protein kinase activity that phosphorylates connexin43 in a pH-dependent manner BJMBR Yahuaca,P.; Ek-Vitorin,J.F.; Rush,P.; Delmar,M.; Taffet,S.M.. The carboxyl-terminal (CT) domain of connexin43 (Cx43) has been implicated in both hormonal and pH-dependent gating of the gap junction channel. An in vitro assay was utilized to determine whether the acidification of cell extracts results in the activation of a protein kinase that can phosphorylate the CT domain. A glutathione S-transferase (GST)-fusion protein was bound to Sephadex beads and used as a target for protein kinase phosphorylation. A protein extract produced from sheep heart was allowed to bind to the fusion protein-coated beads. The bound proteins were washed and then incubated with 32P-ATP. Phosphorylation was assessed after the proteins were resolved by SDS-PAGE. Incubation at pH 7.5 resulted in a minimal amount of phosphorylation while... Tipo: Info:eu-repo/semantics/article Palavras-chave: Connexin; Phosphorylation; Phosphotransferases; Protein kinase. Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000400005 Registros recuperados: 1 Primeira ... 1 ... Última

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