, 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


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.


Enzyme Excited State Glutamine Pyrene Butyrate 
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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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