Fluorescence polarization studies of lysozyme and lysozyme-saccharide complexes

1973 ◽  
Vol 74 (4) ◽  
pp. 519-531 ◽  
Author(s):  
Vivian I. Teichberg ◽  
Meir Shinitzky
Keyword(s):  
Fluorescence Polarization ◽  
Polarization Studies

scholarly journals Fluorescence-polarization studies on binding of 4-methylumbelliferyl β-d-galactopyranoside to Ricinus communis (castor-bean) agglutinin

1980 ◽  
Vol 191 (2) ◽  
pp. 395-400 ◽  
Author(s):  
M I Khan ◽  
M K Mathew ◽  
P Balaram ◽  
A Surolia
Keyword(s):  
Binding Sites ◽  
Fluorescence Polarization ◽  
Castor Bean ◽  
Ricinus Communis ◽  
Equilibrium Dialysis ◽  
Scatchard Analysis ◽  
Polarization Data ◽  
Appreciable Change ◽  
Number Of Binding Sites ◽  
Polarization Studies

The binding of Ricinus communis (castor-bean) agglutinin 1 to saccharides was studied by equilibrium dialysis and fluorescence polarization by using the fluorescently labelled sugar 4-methylumbelliferyl beta-D-galactopyranoside. No appreciable change in ligand fluorescence of 4-methylumbelliferyl beta-D-galactopyranoside was considerably polarized on its binding to the lectin. The association constants obtained by Scatchard analysis of equilibrium-dialysis and fluorescence-polarization data do not differ much from each other, and at 25 degrees C, Ka = 2.4 (+/- 0.2) X 10(4)M-1. These values agree reasonably well with that reported in the literature for Ricinus agglutinin 1. The number of binding sites obtained by the different experimental procedures is 1.94 +/- 0.1 per molecule of 120 000 daltons and is equal to the reported value of 2. The consistency in the values of Ka and number of binding sites indicate the absence of additional subsites on Ricinus agglutinin 1 for its specific sugars. In addition, the excellent agreement between the binding parameters obtained by equilibrium dialysis and fluorescence polarization indicate the potential of ligand-fluorescence-polarization measurements in the investigation of lectin-sugar interactions.

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