Consulta: creatorFacets:"Rush,P."
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Data/hora: 10/06/2024 04:42:14

Identification of a protein kinase activity that phosphorylates connexin43 in a pH-dependent manner
Provedor de dados: Brazilian Journal of Medical and Biological Research
Autores: 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