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  The nature of the stable noncovalent dimers of band 3 protein from erythrocyte membranes in solutions of Triton X-100

Schubert, D., Boss, K., Dorst, H.-J., Flossdorf, J., & Pappert, G. (1983). The nature of the stable noncovalent dimers of band 3 protein from erythrocyte membranes in solutions of Triton X-100. FEBS Letters, 163(1), 81-84. doi:10.1016/0014-5793(83)81168-5.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0008-4AB8-6 Version Permalink: https://hdl.handle.net/21.11116/0000-0008-4AB9-5
Genre: Journal Article

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 Creators:
Schubert, Dieter1, Author           
Boss, Karin1, Author           
Dorst, Hans-Jürgen1, Author           
Flossdorf, J.2, Author
Pappert, Gunter1, Author           
Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              
2Gesellschaft für Biotechnologische Forschung mbH, Braunschweig, Federal Republic of Germany, ou_persistent22              

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Free keywords: Erythrocyte membrane; Band 3 protein; Stable noncovalent dimer; Association equilibrium; Triton X-100; Peroxide
 Abstract: Stable noncovalent dimers of band 3 protein from human erythrocyte membranes, in which state the protein is thought to exist after solubilization by the nonionic detergent Triton X-100, do not occur when purified batches of the detergent are used. Instead, the protein is in a monomer/dimer/tetramer association equilibrium. The stable dimers do appear, however, when the detergent has been 'aged'. They thus seem to be artifacts.

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Language(s): eng - English
 Dates: 1983-09-051983-10-31
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0014-5793(83)81168-5
PMID: 6628694
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 163 (1) Sequence Number: - Start / End Page: 81 - 84 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501