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

Passow, Hermann; Fasold, Hugo; Lepke, Sigrid; Pring, M.; Schuhmann, B.

doi:10.1007/978-1-4684-3279-4_17

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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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Item Permalink: https://hdl.handle.net/21.11116/0000-0008-E431-F Version Permalink: https://hdl.handle.net/21.11116/0000-0008-E432-E

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: Date issued: 1977

Publication Status: Issued

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