Functional demonstration of connexin-protein binding using surface plasmon resonance.
Cell Commun Adhes
; 8(4-6): 225-9, 2001.
Article
en En
| MEDLINE
| ID: mdl-12064593
Surface plasmon resonance (SPR) allows examination of protein-protein interactions in real time, from which both binding affinities and kinetics can be directly determined. We have used the SPR technique to search for proteins in heart tissue that would be candidate binding partners for the cardiac gap junction protein, connexin43 (Cx43). Heart lysate showed a strong, pH-dependent binding to the carboxyl terminus (CT) of Cx43 (amino acids 254-382) covalently linked to an SPR cuvette. Binding was inhibited by the presence of v-src transfected 3T3 cell lysate, suggesting that binding partners in these two lysates may compete for overlapping epitopes on Cx43CT. The combined application of proteomic and functional studies is expected to identify which proteins within heart tissue interact with Cx43 and what roles they may play in gap junction function.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Conexina 43
/
Resonancia por Plasmón de Superficie
/
Miocardio
Límite:
Animals
Idioma:
En
Revista:
Cell Commun Adhes
Año:
2001
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Reino Unido