Literature DB >> 2579684

Simple model can explain self-inhibition of red cell anion exchange.

C Tanford.   

Abstract

Ion translocation in red cell anion exchange is assumed to occur by means of an alternating access mechanism, in which a critical binding site for the transported ion alternates between two conformational states, each accessible from only one side of the membrane. If this alternating site is located within the transport protein at some distance from one or both surfaces of the membrane, an access channel is required to connect the alternating site to the adjacent bulk solution. This automatically leads to inhibition of transport at high concentrations of the transported ion because release of the ion from the alternating site can occur only via unoccupied channel sites.

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Year:  1985        PMID: 2579684      PMCID: PMC1435073          DOI: 10.1016/S0006-3495(85)83871-6

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  12 in total

1.  Kinetic characteristics of the sulfate self-exchange in human red blood cells and red blood cell ghosts.

Authors:  K F Schnell; S Gerhardt; A Schöppe-Fredenburg
Journal:  J Membr Biol       Date:  1977-01-28       Impact factor: 1.843

2.  A channel mechanism for electrogenic ion pumps.

Authors:  P Läuger
Journal:  Biochim Biophys Acta       Date:  1979-03-23

3.  Simple model for the chemical potential change of a transported ion in active transport.

Authors:  C Tanford
Journal:  Proc Natl Acad Sci U S A       Date:  1982-05       Impact factor: 11.205

Review 4.  Mechanism of free energy coupling in active transport.

Authors:  C Tanford
Journal:  Annu Rev Biochem       Date:  1983       Impact factor: 23.643

5.  Translocation pathway in the catalysis of active transport.

Authors:  C Tanford
Journal:  Proc Natl Acad Sci U S A       Date:  1983-06       Impact factor: 11.205

6.  Location of the stilbenedisulfonate binding site of the human erythrocyte anion-exchange system by resonance energy transfer.

Authors:  A Rao; P Martin; R A Reithmeier; L C Cantley
Journal:  Biochemistry       Date:  1979-10-16       Impact factor: 3.162

7.  Phosphate transport in human red blood cells: concentration dependence and pH dependence of the unidirectional phosphate flux at equilibrium conditions.

Authors:  K F Schnell; E Besl; R von der Mosel
Journal:  J Membr Biol       Date:  1981       Impact factor: 1.843

8.  Evidence that inhibitors of anion exchange induce a transmembrane conformational change in band 3.

Authors:  I G Macara; S Kuo; L C Cantley
Journal:  J Biol Chem       Date:  1983-02-10       Impact factor: 5.157

9.  Effects of halides and bicarbonate on chloride transport in human red blood cells.

Authors:  M Dalmark
Journal:  J Gen Physiol       Date:  1976-02       Impact factor: 4.086

10.  Asymmetry in the mechanism for anion exchange in human red blood cell membranes. Evidence for reciprocating sites that react with one transported anion at a time.

Authors:  R B Gunn; O Fröhlich
Journal:  J Gen Physiol       Date:  1979-09       Impact factor: 4.086

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  4 in total

1.  Inhibition of the phosphate self-exchange flux in human erythrocytes and erythrocyte ghosts.

Authors:  F Stadler; K F Schnell
Journal:  J Membr Biol       Date:  1990-10       Impact factor: 1.843

Review 2.  The "tunneling" mode of biological carrier-mediated transport.

Authors:  O Fröhlich
Journal:  J Membr Biol       Date:  1988-03       Impact factor: 1.843

3.  Denaturation of a membrane transport protein by urea: the erythrocyte anion exchanger.

Authors:  O Fröhlich; S C Jones
Journal:  J Membr Biol       Date:  1987       Impact factor: 1.843

4.  Identification of multiple substrate binding sites in SLC4 transporters in the outward-facing conformation: insights into the transport mechanism.

Authors:  Hristina R Zhekova; Alexander Pushkin; Gülru Kayık; Liyo Kao; Rustam Azimov; Natalia Abuladze; Debra Kurtz; Mirna Damergi; Sergei Noskov; Ira Kurtz
Journal:  J Biol Chem       Date:  2021-04-28       Impact factor: 5.157

  4 in total

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