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  The effects of dansylation on the pH dependence of SO42− and Cl equilibrium exchange and on the H+/SO42−cotransport across the red blood cell membrane

Berghout, A. G., Raida, M., Legrum, B., & Passow, H. (1989). The effects of dansylation on the pH dependence of SO42− and Cl equilibrium exchange and on the H+/SO42−cotransport across the red blood cell membrane. Biochimica et Biophysica Acta-Biomembranes, 986(1), 75-82. doi:10.1016/0005-2736(89)90274-5.

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 Creators:
Berghout, Alexander G.R.V.1, Author           
Raida, Manfred1, Author           
Legrum, Barbara1, Author           
Passow, Hermann1, Author           
Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              

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Free keywords: Anion transport; Erythrocyte membrane; Dansyl chloride; Band 3 protein; Cotransport
 Abstract: Treatment of the erythrocyte membrane with dansyl chloride leads to the following effects: (i) SO42− transport is enhanced, Cl transport is reduced. At maximal acceleration of sulfate exchange, Cl exchange is only partially inhibited. The two effects are lineary related suggesting that the Cl and SO42− transporting forms of band 3 are derived from the same pool. (ii) The maximum of the pH dependence of SO42− equilibrium exchange as measured at low sulfate concentrations is replaced by a plateau. It now resembles the pH dependence of Cl exchange in untreated red cells. The pH dependence of SO42− equilibrium exchange as measured at high sulfate concentrations is virtually unchanged after dansylation. The pH dependence of the partially inhibited Cl equilibrium exchange across the dansylated membrane as measured at high chloride concentrations remains similar as in the untreated red cells but is somewhat less pronounced. (iii) SO42−/H+ cotransport remains essentially unaltered after modification by dansyl chloride. The effects of dansylation are discussed in terms of a model similar to the titratable carrier model originally proposed by Gunn (Gunn, R.B. (1972) in Oxygen Affinity of Hemoglobin and Red Cell Acid Base Status (Rorth, M. and Astrup, P., eds.), pp. 823–827, Munksgaard, Copenhagen).

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Language(s): eng - English
 Dates: 1989-07-211989-03-232003-03-311989-11-17
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0005-2736(89)90274-5
PMID: 2819098
 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: 986 (1) Sequence Number: - Start / End Page: 75 - 82 Identifier: ISSN: 0005-2736
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702