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Experientia

, Volume 33, Issue 8, pp 1016–1018 | Cite as

Interaction of extrinic fluoresence probes with E. coli glutamine synthetase

  • F. C. Wedler
  • B. A. Willis
  • R. Srubas
Specialia Chimica, Biochimica

Summary

Binding of 2-p-toluidinylnaphthalene-6-sulfonate (TNS) to adenylylated\(E_{\overline {11} } \) glutamine synthetase is cooperative and time-dependent, with 3 dye sites per subunit. In fluorescence polarization experiments TNS and pyrene butyrate give normalized Perrin plots that indicate a symmetrical arrangement of dye excited state dipoles, relative to the rotational axis of the oblate ellipsoid of the dodecameric native enzyme.

Keywords

Enzyme Excited State Glutamine Pyrene Butyrate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Birkhäuser Verlag 1977

Authors and Affiliations

  • F. C. Wedler
    • 1
  • B. A. Willis
    • 1
  • R. Srubas
    • 1
  1. 1.Biochemistry Program, Chemistry Departement, Cogswell LaboratoryRensselaer Polytechnic InstituteTroyUSA)

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