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  The Action of 2-(4′-Amino Phenyl)-6-Methyl Benzene Thiazol-3,7′-Disulfonic Acid (APMB) on Anion Transport and the Protein in Band 3 of the Red Blood Cell Membrane

Passow, H., Pring, M., Legrum, B., & Zaki, L. (1977). The Action of 2-(4′-Amino Phenyl)-6-Methyl Benzene Thiazol-3,7′-Disulfonic Acid (APMB) on Anion Transport and the Protein in Band 3 of the Red Blood Cell Membrane. In G. Semenza, & E. Carafoli (Eds.), Biochemistry of Membrane Transport. Proceedings in Life Science (pp. 306-315 ). Berlin, Heidelberg: Springer-Verlag 1977.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0009-80CD-F Version Permalink: https://hdl.handle.net/21.11116/0000-0009-80CE-E
Genre: Conference Paper

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 Creators:
Passow, Hermann1, Author           
Pring, M.1, Author           
Legrum, Barbara1, Author           
Zaki, Laila1, Author           
Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              

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 Abstract: The disulfonic acid APMB produces maximally about 85% inhibition of sulfate equilibrium exchange. Inhibition is half maximal at about 0.4 mM APMB. The reversibly binding APMB shares binding sites with the irreversibly binding inhibitors DNFB and H2DIDS on the protein in band 3 and on the anion transport system. This was demonstrated by observing the inhibitory effect of increasing concentrations of APMB on the rate of dinitrophenylation of common binding sites of DNFB and H2DIDS on band 3 and on the anion transport system. A mathematical description of the effect of APMB on dinitrophenylation of the anion transport system was consistent with the assumption that APMB reacts with 85% of the DNFB binding sites with a Km value which is close to the KI value observed in studies of the inhibitory effect of APMB.

An investigation of the effects of increasing sulfate concentration on sulfate transport showed, in accordance with previous work of Schnell (1975), that the sulfate flux passes through a maximum which suggests the existence of an inhibitory modifier site in addition to a transfer site. Inhibition by APMB decreases slightly over the sulfate concentration range 30 to 300 mM, with half maximal inhibition at APMB concentrations of 0.9 and 0.4 mM, respectively, at the upper and lower limits of this concentration range. The inferred low affinity of SO4 for modifier and transfer sites and the variations of ionic strength associated with variations of sulfate concentration made it impossible to decide whether sulfate reduces inhibition by a specific reaction with one or both of the two sites, or by other interactions not involving specific binding sites.

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Language(s): eng - English
 Dates: 1977
 Publication Status: Issued
 Pages: 20
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/978-3-642-66564-6_22
 Degree: -

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Title: FEBS Symposium on the Biochemistry of Membrane Transport
Place of Event: Swiss Institute of Technology, Zürich
Start-/End Date: 1976-07-18 - 1976-07-23

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Title: Biochemistry of Membrane Transport. Proceedings in Life Science
  Subtitle : FEBS — Symposium No. 42
Source Genre: Proceedings
 Creator(s):
Semenza, Giorgio1, Editor
Carafoli, Ernesto1, Editor
Affiliations:
1 Laboratorium für BiochemieEidgenössische Technische Hochschule ZürichZürichSwitzerland, ou_persistent22            
Publ. Info: Berlin, Heidelberg : Springer-Verlag 1977
Pages: 669 Volume / Issue: - Sequence Number: - Start / End Page: 306 - 315 Identifier: DOI: 10.1007/978-3-642-66564-6
ISBN: 978-3-642-66566-0
ISBN: 978-3-642-66564-6