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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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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0008-E431-F Versions-Permalink: https://hdl.handle.net/21.11116/0000-0008-E432-E
Genre: Konferenzbeitrag

Externe Referenzen

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Urheber

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 Urheber:
Passow, Hermann1, Autor           
Fasold, Hugo2, Autor
Lepke, Sigrid1, Autor           
Pring, M.1, Autor           
Schuhmann, B.1, Autor           
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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Schlagwörter: -
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 1977
 Publikationsstatus: Erschienen
 Seiten: 27
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1007/978-1-4684-3279-4_17
PMID: 899952
 Art des Abschluß: -

Veranstaltung

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Titel: Proceedings of the Ninth Annual Rochester International Conference on Environmental Toxicity
Veranstaltungsort: Rochester, New York
Start-/Enddatum: 1976-05-24 - 1976-05-26

Entscheidung

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Projektinformation

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Quelle 1

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Titel: Advances in Experimental Medicine and Biology
  Untertitel : Membrane Toxicity
Genre der Quelle: Reihe
 Urheber:
Miller , Morten W.1, Herausgeber
Shamoo, Adil E.1, Herausgeber
Affiliations:
1 The University of Rochester, Rochester, USA, ou_persistent22            
Ort, Verlag, Ausgabe: Boston, MA, USA : Springer-Verlag US
Seiten: 553 Band / Heft: 84 Artikelnummer: - Start- / Endseite: 353 - 379 Identifikator: DOI: 10.1007/978-1-4684-3279-4
ISBN: 978-1-4684-3281-7