Literature DB >> 2947628

Distances between the functional sites of sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase and the lipid/water interface.

J A Teruel, J C Gómez-Fernández.   

Abstract

Measurements of fluorescence energy transfer have been performed to determine the distance between the lipid-water interface and the ATP-binding site in the (Ca2+ + Mg2+)-ATPase from sarcoplasmic reticulum. The calculated distance between the donor, FITC bound to the protein (nucleotide binding-site marker), and the acceptor, rhodamine-5'-isothiocyanyldipalmitoylphosphatidylethanolamine (RITC-DPPE) incorporated in the membrane, was in the range of 34-42 A. In addition the distance between the high affinity Ca2+-binding sites and the lipid/water interface has been calculated by luminescence energy transfer from Tb3+ bound to the Ca2+ sites to RITC-DPPE included in the membrane, and it was approx. 10 A.

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Year:  1986        PMID: 2947628     DOI: 10.1016/0005-2736(86)90257-9

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  4 in total

1.  The ATP-binding site of Ca(2+)-ATPase revealed by electron image analysis.

Authors:  K Yonekura; D L Stokes; H Sasabe; C Toyoshima
Journal:  Biophys J       Date:  1997-03       Impact factor: 4.033

Review 2.  Molecular tools to elucidate problems in excitation-contraction coupling.

Authors:  D H MacLennan
Journal:  Biophys J       Date:  1990-12       Impact factor: 4.033

3.  Involvement of an arginyl residue in the nucleotide-binding site of Ca(2+)-ATPase from sarcoplasmic reticulum as seen by reaction with phenylglyoxal.

Authors:  S Corbalán-García; J A Teruel; J C Gómez-Fernández
Journal:  Biochem J       Date:  1996-08-15       Impact factor: 3.857

4.  Labelling the Ca(2+)-ATPase of skeletal-muscle sarcoplasmic reticulum with the cross-linker o-phthalaldehyde.

Authors:  Y M Khan; M Wictome; J M East; A G Lee
Journal:  Biochem J       Date:  1996-07-15       Impact factor: 3.857

  4 in total

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