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  Photo-activated inhibition of sulfate equilibrium exchange in human erythrocyte ghosts by a 4-azido-2-nitrobenzoate derivative of phlorizin

Kaplan, J. H., & Fasold, H. (1976). Photo-activated inhibition of sulfate equilibrium exchange in human erythrocyte ghosts by a 4-azido-2-nitrobenzoate derivative of phlorizin. Biochimica et Biophysica Acta-Biomembranes, 443(3), 525-533. doi:10.1016/0005-2736(76)90470-3.

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 Creators:
Kaplan, Jack H.1, Author           
Fasold, Hugo2, Author
Affiliations:
1Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              
2Institut für Biochemie, Goethe-Universität Frankfurt, Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: ANB-phlorizin4-azido-2-nitrobenzoate glycoside of phlorizin; NB-phlorizin2-nitrobenzoate glycoside of phlorizin; DAS4,4′-diacetamidostilbene-2,2′-disulfonic acid
 Abstract: Like phlorizin, two glycosidic esters of phlorizin, the 4-azido-2-nitrobenzoate (ANB-phlorizin) and the 2-nitrobenzoate (NB-phlorizin) were found to be effective inhibitors of SO42− equilibrium exchange at the outer but not at the inner membrane surface of the human erythrocyte ghost. After photolysis of ghost suspensions in the presence of extracellular ANB-phlorizin an irreversible inhibition of SO42− exchange was observed, while photolysis of intracellular ANB-phlorizin was without effect. After photolysis in the presence of extracellular or intracellular tritiated ANB-phlorizin gel electrophoresis of the labelled membranes revealed similar locations of binding. These findings suggest that the sidedness of action of ANB-phlorizin could not be related to inaccessibility of the inner membrane surface for the agent but that inhibition occurs via binding to fixed sites at the outer membrane surface that are not associated with a mobile carrier which crosses the membrane.

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Language(s): eng - English
 Dates: 1976-02-112003-03-241976-09-07
 Publication Status: Issued
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0005-2736(76)90470-3
 Degree: -

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Title: Biochimica et Biophysica Acta-Biomembranes
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 443 (3) Sequence Number: - Start / End Page: 525 - 533 Identifier: ISSN: 0005-2736
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702