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  Three different actions of phenylglyoxal on band 3 protein-mediated anion transport across the red blood cell membrane

Gärtner, E.-M., Liebold, K. M., Legrum, B., Fasold, H., & Passow, H. (1997). Three different actions of phenylglyoxal on band 3 protein-mediated anion transport across the red blood cell membrane. Biochimica et Biophysica Acta-Biomembranes, 1323(2), 208-222. doi:10.1016/S0005-2736(96)00187-3.

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 Creators:
Gärtner, Eva-Maria1, Author           
Liebold, Katja M.2, Author
Legrum, Barbara1, Author           
Fasold, Hugo3, Author
Passow, Hermann4, Author           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Institute for Animal Physiology, Justus-Liebig-University, D-35392 Giessen, Germany, ou_persistent22              
3Institute of Biochemistry, Goethe-University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              
4Emeritusgroup Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3273412              

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Free keywords: Sulfate transport; AE1; Erythrocyte membrane; Arginine
 Abstract: Phenylglyoxalation of the red blood cell membrane leads to three superimposed effects on band 3 protein-mediated anion equilibrium exchange as measured by means of radiosulfate: (1) a shift of the curve relating transport activity to pH towards lower pH values, possibly in combination with an increase of the maximal transport activity. This is accompanied by effect (2), the abolishment of a chloride-stimulated component of anion transport seen at low pH values. Effect (3) consists of inhibition of anion equilibrium exchange. Effect (1) prevails when phenylglyoxalation is performed at low concentrations of PG and low pH, while effect (3) predominates when exposure to PG is executed at high pH and high concentration of PG. Effect (1) is associated with a decrease of the Ki values for inhibition and binding of the reversibly acting stilbene disulfonates DNDS and DBDS. The inhibition observed as a consequence of effect (3) is linearly related to a decrease of the capacity of band 3 to combine with the stilbene disulfonate DBDS. The results are interpreted on the assumption that PG is capable of reacting with two or possibly three distinct binding sites in band 3. Reaction with one of them leads to effect (1) and, perhaps, to effect (2); reaction with the other to effect (3). The latter is possibly due to modification of Arg 730, which is homologous to Arg 748 in mouse band 3. Site-directed mutagenesis of this arginine residue showed that it is required for band 3-mediated anion transport.

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Language(s): eng - English
 Dates: 1996-09-111996-05-291996-09-121998-01-201997-01-31
 Publication Status: Published in print
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0005-2736(96)00187-3
PMID: 9042344
 Degree: -

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Title: Biochimica et Biophysica Acta-Biomembranes
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1323 (2) Sequence Number: - Start / End Page: 208 - 222 Identifier: ISSN: 0005-2736
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702