Dynamics ofLens culinaris agglutinin studied by red-edge excitation spectra and anisotropy measurements of 2-p-toluidinylnaphthalene-6-sulfonate (TNS) and of tryptophan residues

Abstract The fluorescence of 2-p-toluidinylnaphthalene-6-sulfonate bound toLens culinaris agglutinin and of the Trp residues of the protein was investigated. Red-edge excitation spectra and steady-state anisotropy as a function of temperature indicate that the TNS is bound rigidly. Red-edge excitati...

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Bibliographic Details
Published in:Journal of fluorescence, Vol. 6 (1996), p. 199-208
Other Involved Persons: Albani, J. R.
Format: electronic Article
Item Description:Copyright: Copyright 1996 Plenum Publishing Corporation
Physical Description:Online-Ressource
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