Evidence for the asymmetrical binding of p-chloromercuriphenyl sulphonate to the human erythrocyte nucleoside transporter

Chung Ming Tse, Jin Shyun R Wu, James D. Young

Research output: Contribution to journalArticle

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 μM), 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.

Original languageEnglish (US)
Pages (from-to)316-324
Number of pages9
JournalBBA - Biomembranes
Volume818
Issue number3
DOIs
StatePublished - Sep 10 1985
Externally publishedYes

Fingerprint

4-Chloromercuribenzenesulfonate
Nucleoside Transport Proteins
Erythrocytes
Uridine
Erythrocyte Membrane
Membranes
Facilitated Diffusion
Dithiothreitol
Nucleosides
Cell Membrane
4-nitrobenzylthioinosine

Keywords

  • Chemical asymmetry
  • Erythrocyte membrane
  • Nucleoside transport
  • p-Chloromercuriphenyl sulfonate (PCMBS)

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology

Cite this

Evidence for the asymmetrical binding of p-chloromercuriphenyl sulphonate to the human erythrocyte nucleoside transporter. / Tse, Chung Ming; Wu, Jin Shyun R; Young, James D.

In: BBA - Biomembranes, Vol. 818, No. 3, 10.09.1985, p. 316-324.

Research output: Contribution to journalArticle

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