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  A conformational transition of the sarcoplasmic reticulum calcium transport ATPase induced by vanadate

Hasselbach, W., Medda, P., Migala, A., & Agostini, B. (1983). A conformational transition of the sarcoplasmic reticulum calcium transport ATPase induced by vanadate. Zeitschrift für Naturforschung, C: Journal of Biosciences, 38(11-12), 1015-1022. doi:10.1515/znc-1983-11-1223.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0003-693E-3 Version Permalink: https://hdl.handle.net/21.11116/0000-0003-693F-2
Genre: Journal Article

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 Creators:
Hasselbach, Wilhelm1, Author           
Medda, Pankaj2, Author           
Migala, Andrea3, Author           
Agostini, Bruno3, Author           
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              
3Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497699              

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 Abstract: Vanadate binding to sarcoplasmic reticulum vesicles results in the loss of the externally located high affinity calcium binding sites of the calcium transport ATPase. Conversely the occupation by calcium of the internally located low affinity sites in the vanadate enzyme complex leads to the release of vanadate. Since the total number of calcium binding sites is not diminished by vanadate binding but slightly increases we conclude that vanadate binding induces a transition of the enzymes external high to internal low affinity calcium binding sites. The transposition of external to internal calcium binding sites is accompanied by a definite change in the structure of the sarcoplasmic reticulum membranes. On vanadate binding the asymmetrically arranged electron dense protein particles become symmetrically distributed.

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Language(s): eng - English
 Dates: 1983-09-142014-06-021983-12-01
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1515/znc-1983-11-1223
URI: https://www.ncbi.nlm.nih.gov/pubmed/6230804
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Title: Zeitschrift für Naturforschung, C: Journal of Biosciences
  Abbreviation : Z. Naturforsch., C: J. Biosci.
Source Genre: Journal
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Publ. Info: Berlin : Walter de Gruyter GmbH
Pages: - Volume / Issue: 38 (11-12) Sequence Number: - Start / End Page: 1015 - 1022 Identifier: ISSN: 1865-7125
CoNE: https://pure.mpg.de/cone/journals/resource/954927655916_1