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  Mediation of inorganic anion transport by the hydrophobic domain of mouse erythroid band 3 protein expressed in oocytes of Xenopus laevis

Lepke, S., Becker, A., & Passow, H. (1992). Mediation of inorganic anion transport by the hydrophobic domain of mouse erythroid band 3 protein expressed in oocytes of Xenopus laevis. Biochimica et Biophysica Acta-Biomembranes, 1106(1), 13-16. doi:10.1016/0005-2736(92)90215-8.

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 Creators:
Lepke, Sigrid1, Author           
Becker, Anja1, 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: Band 3 protein; Anion transport; cDNA; Chloride transport; (Mouse erythroid); (Xenopus oocyte)
 Abstract: A cDNA clone of the mouse erythroid band 3 protein encoding the 556 amino acid residues of the hydrophobic domain from Thr-374 to the C-terminal Val-929 is shown by immunoprecipitation to be expressed in Xenopus oocytes. Measurements of 36Cl- efflux indicate that the translation product mediates Cl- transport, which is inhibitable reversibly by DNDS or H2DIDS, specific inhibitors of band 3-mediated transport. The apparent KI values are 3.6 microM and 0.094 microM, respectively, and hence similar to those found in the wild type band 3-mediated anion transport. The rapid reversible inhibition by H2DIDS slowly changes to irreversible inhibition. The rate of change increases with increasing pH, again similar as to the wild-type band 3. It is concluded that the hydrophobic domain of band 3 is capable of executing anion transport essentially similar to the full-length band 3, although minor differences with respect to transport and inhibition kinetics cannot be ruled out.

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Language(s): eng - English
 Dates: 1991-07-121992-04-29
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0005-2736(92)90215-8
PMID: 1581325
 Degree: -

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Title: Biochimica et Biophysica Acta-Biomembranes
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1106 (1) Sequence Number: - Start / End Page: 13 - 16 Identifier: ISSN: 0005-2736
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702