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  Chemical and enzymatic modification of membrane proteins and anion transport in human red blood cells

Passow, H., Fasold, H., Lepke, S., Pring, M., & Schuhmann, B. (1977). Chemical and enzymatic modification of membrane proteins and anion transport in human red blood cells. Boston, MA, USA: Springer-Verlag US.

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Genre: Conference Paper

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 Creators:
Passow, Hermann1, Author           
Fasold, Hugo2, Author
Lepke, Sigrid1, Author           
Pring, M.1, Author           
Schuhmann, B.1, Author           
Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              
2Biochemisches Institut, Johann Wolfgang Goethe-Universität Frankfurt, Frankfurt am Main, Germany, ou_persistent22              

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 Abstract: The paper is introduced by a review of the developments which lead to the suggestion of an involvement of the protein in band 3 (nomenclature of Steck, ref.2) in anion transport across the red cell membrane. Subsequently, it is shown that DIDS and its dihydroderivative H2DIDS, which both played an essential role in the reviewed work, not only combine with the protein in band 3 but also with other membrane constituents. At maximal inhibition 1.1–1.3 molecules of DIDS or H2DIDS are bound per molecule of protein in band 3. Combined treatment with 3h pDIDS and esternai chymotrypsin, pronase or papain demonstrates the existence of peptides in the protein in band 3 which differ with respect to their accessibility or susceptibility to proteolysis. Each enzyme affects the protein differently and produces different changes of anion transport. In contrast to external trypsin which has neither an effect on the protein in band 3 nor on anion transport, internal trypsin splits the protein in band 3 completely. Fragments of 58,000 and 48,000 Daltons remain attached to the membrane while other products of hydrolysis are released into the medium. Anion transport is partially inhibited but continues to exhibit the essential features seen in the intact cell. The described results are compatible with an involvement of some component of the protein in band 3 in anion transport. They show that additional evidence is required to provide more definitive proof of such involvement.

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Language(s): eng - English
 Dates: 1977
 Publication Status: Published in print
 Pages: 27
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/978-1-4684-3279-4_17
PMID: 899952
 Degree: -

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Title: Proceedings of the Ninth Annual Rochester International Conference on Environmental Toxicity
Place of Event: Rochester, New York
Start-/End Date: 1976-05-24 - 1976-05-26

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Title: Advances in Experimental Medicine and Biology
  Subtitle : Membrane Toxicity
Source Genre: Series
 Creator(s):
Miller , Morten W.1, Editor
Shamoo, Adil E.1, Editor
Affiliations:
1 The University of Rochester, Rochester, USA, ou_persistent22            
Publ. Info: Boston, MA, USA : Springer-Verlag US
Pages: 553 Volume / Issue: 84 Sequence Number: - Start / End Page: 353 - 379 Identifier: DOI: 10.1007/978-1-4684-3279-4
ISBN: 978-1-4684-3281-7