Identification by site-directed mutagenesis of Lys-558 as the covalent 
attachment site of H2DIDS in the mouse erythroid band 3 protein

Bartel, Detlef; Hans, Heidrun; Passow, Hermann

doi:10.1016/0005-2736(89)90427-6

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Identification by site-directed mutagenesis of Lys-558 as the covalent attachment site of H₂DIDS in the mouse erythroid band 3 protein

Bartel, D., Hans, H., & Passow, H. (1989). Identification by site-directed mutagenesis of Lys-558 as the covalent attachment site of H₂DIDS in the mouse erythroid band 3 protein. Biochimica et Biophysica Acta-Biomembranes, 985(3), 355-358. doi:10.1016/0005-2736(89)90427-6.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0007-CD4A-0 Version Permalink: https://hdl.handle.net/21.11116/0000-0007-CD4B-F

Genre: Journal Article

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Creators:
Bartel, Detlef¹, Author
Hans, Heidrun¹, 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; cRNA expression; Oligonucleotide-directed; mutagenesis; Inhibitor binding site; (Xenopus oocyte)

Abstract: After functional expression of mouse erythroid band 3 by cRNA microinjection into Xenopus oocytes, ³⁶Cl⁻ efflux is irreversibly inhibited by H₂DIDS. When a cRNA is injected that is derived from a cDNA in which the nucleotides encoding for lysine-558 were replaced by nucleotides encoding for asparagine, transport and inhibition of transport by H₂DIDS still occur. However, when measured under conditions where no intramolecular crosslinking takes place the inhibition by H₂DIDS is no longer irreversible. This indicates that thiourea bond formation between H₂DIDS and band 3 takes place at Lys-558.

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Language(s): eng - English

Dates: Submitted: 1989-07-13Published Online: 2003-03-21Date issued: 1989-11-03

Publication Status: Issued

Pages: 4

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Table of Contents: -

Rev. Type: Peer

Identifiers: DOI: 10.1016/0005-2736(89)90427-6

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Title: Biochimica et Biophysica Acta-Biomembranes

Source Genre: Journal

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Publ. Info: Amsterdam : Elsevier

Pages: - Volume / Issue: 985 (3) Sequence Number: - Start / End Page: 355 - 358 Identifier: ISSN: 0005-2736
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702