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  Inhibition of anion transport in the human red blood cell membrane with para- and meta-methoxyphenylglyoxal

Betakis, E., Fritzsch, G., & Zaki, L. (1992). Inhibition of anion transport in the human red blood cell membrane with para- and meta-methoxyphenylglyoxal. Biochimica et Biophysica Acta, Bioenergetics, 1110(1), 75-80. doi:10.1016/0005-2736(92)90296-x.

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 Creators:
Betakis, Evlampios1, Author              
Fritzsch, Günter2, Author              
Zaki, Laila1, Author              
Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: Band 3; Arginine residue; Anion binding site; (Human)
 Abstract: The positional isomers para-methoxyphenylglyoxal and meta-methoxyphenylglyoxal were newly synthesized and found to be potent inhibitors of sulfate exchange in the red blood cell membrane. The rate of inactivation of the transport system with both reagents obeys pseudo-first-order kinetics and increases with increasing pH and reagent concentration. The degree of inhibition of the transport system with the meta-isomer exceeds the inhibition caused by the para-isomer. At 2 mM 3-methoxyphenylglyoxal (3-MOPG) and 37 degrees C the half-lifetime of the anion transporter is 5.4 min at pH 8.0. Under the same experimental conditions the half-lifetime of the transporter at 2 mM 4-methoxyphenylglyoxal (4-MOPG) is found to be 24.7 min. The binding site of these reagents is found to be the same as binding site of the reversibly acting phenylglyoxal derivative 4-hydroxy-3-nitrophenylglyoxal (HNPG). Chloride ions are able to protect the transporter against inhibition with both reagents. Anion transport inhibitors like 4,4'-dinitrostilbene-2,2'-disulfonate (DNDS) and flufenemate, which are known to act on band 3 protein, are able to interact with the binding of the newly synthesised reagents. Phloretin and phloridzin show no interaction.

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Language(s): eng - English
 Dates: 1992-04-062003-03-311992-09-21
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0005-2736(92)90296-x
PMID: 139083
 Degree: -

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Title: Biochimica et Biophysica Acta, Bioenergetics
  Abbreviation : Biochim. Biophys. Acta, Bioenerg.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1110 (1) Sequence Number: - Start / End Page: 75 - 80 Identifier: ISSN: 0005-2728
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_6