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  Anion transport across the red blood cell membrane and the conformation of the protein in Band 3

Passow, H., Fasold, H., Gärtner, E.-M., Legrum, B., Ruffing, W., & Zaki, L. (1980). Anion transport across the red blood cell membrane and the conformation of the protein in Band 3. Annals of the New York Academy of Sciences, 341, 361-383. doi:10.1111/j.1749-6632.1980.tb47184.x.

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Genre: Journal Article

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 Creators:
Passow, Hermann1, Author           
Fasold, Hugo2, Author
Gärtner, Eva-Maria1, Author           
Legrum, Barbara1, Author           
Ruffing, W.1, Author           
Zaki, Laila1, Author           
Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              
2Biochemisches Institut, Goethe-Universität Frankfurt, D‐6000 Frankfurt am Main 71, West Germany, ou_persistent22              

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 Abstract: Measuring the rate of dinitrophenylation of a specific lysine residue (called a) that is allosterically linked to the transfer site, it could be demonstrated that the anion transport protein may exist in two different conformational states, designated cis and trans. In the cis conformation a is easily accessible for reaction with dinitrofluorobenzene; in the trans conformation, a is less accessible. In the presence of the substrate anion Cl, the equilibrium between the cis and trans conformation is towards the cis conformation. Reversibly acting inhibitors of anion transport arrest the transport system, either predominantly in the cis or in the trans conformation. Phlorizin and certain positively charged derivatives of furosemide produce arrest in cis conformation, internal 2-(4'-aminophenyl)-6-methylbenzenethiazol-3',7-disulfonate (APMB) and Ca++ in trans conformation. Within this frame of reference, the different susceptibilities of the transfer site to internal and external 4,4' diacetamido-2,2'-stilbene disulfonate (DAS) are interpreted on the assumption that the conformation of the transfer site changes during the transition of the transport protein from the cis to the trans conformation, so that in the trans conformation a reaction with DAS is no longer possible.

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Language(s): eng - English
 Dates: 2006-12-161980
 Publication Status: Published in print
 Pages: 23
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1111/j.1749-6632.1980.tb47184.x
PMID: 6772068
 Degree: -

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Title: Annals of the New York Academy of Sciences
  Other : Ann. N.Y. Acad. Sci.
Source Genre: Journal
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Publ. Info: New York : New York Academy of Sciences
Pages: - Volume / Issue: 341 Sequence Number: - Start / End Page: 361 - 383 Identifier: ISSN: 0077-8923
CoNE: https://pure.mpg.de/cone/journals/resource/954926958894_2