Evidence for the asymmetrical binding of p-chloromercuriphenyl sulphonate to the human erythrocyte nucleoside transporter.
Biochim Biophys Acta
; 818(3): 316-24, 1985 Sep 10.
Article
em En
| MEDLINE
| ID: mdl-2994728
ABSTRACT
Nucleosides cross the human erythrocyte membrane by a facilitated-diffusion process which is selectively inhibited by nanomolar concentrations of nitrobenzylthioinosine (NBMPR). The chemical asymmetry of the transporter was investigated by studying the effects of p-chloromercuriphenyl sulphonate (PCMBS) on uridine transport and high-affinity NBMPR binding in inside-out and right-side-out membrane vesicles, unsealed erythrocyte ghosts and intact cells. PCMBS was an effective inhibitor of the transporter (50% inhibition at 30 microM), but only when the organomercurial had access to the cytoplasmic membrane surface. PCMBS inhibition of NBMPR binding to ghosts was reversed by incubation with dithiothreitol. Both uridine and NBMPR were able to protect the transporter against PCMBS inhibition.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Compostos de Fenilmercúrio
/
Proteínas Sanguíneas
/
4-Cloromercuriobenzenossulfonato
/
Proteínas de Membrana
Limite:
Humans
Idioma:
En
Ano de publicação:
1985
Tipo de documento:
Article