Determination of association constants at moderately fast chemical exchange: Complexation of camphor enantiomers by α-cyclodextrin

2006 ◽  
Vol 181 (2) ◽  
pp. 304-309 ◽  
Author(s):  
Piotr Bernatowicz ◽  
Michał Nowakowski ◽  
Helena Dodziuk ◽  
Andrzej Ejchart
PLoS ONE ◽  
2010 ◽  
Vol 5 (2) ◽  
pp. e8943 ◽  
Author(s):  
Janarthanan Krishnamoorthy ◽  
Victor C. K. Yu ◽  
Yu-Keung Mok

1985 ◽  
Vol 229 (3) ◽  
pp. 687-692 ◽  
Author(s):  
F Tabary ◽  
J P Frénoy

The interaction of lectin isolated from rice (Oryza sativa) embryos with N-acetylglucosaminides was studied by equilibrium dialysis and fluorescence. Equilibrium dialysis with 4-methylumbelliferyl-(GlcNac)2 showed that rice lectin (Mr 38000) contains four equivalent saccharide-binding sites. Addition of the N-acetylglucosaminides GlcNac, (GlcNac)2 and (GlcNac)3 enhanced the intrinsic fluorescence of rice lectin and this was accompanied by a 10nm blue-shift of its maximum fluorescence with (GlcNac)2 and (GlcNac)3. These changes in intensity allowed determination of the association constants, which increased with the number of saccharide units: at 20 degrees C, Ka = (1.3 +/- 0.1) X 10(3), (5.1 +/- 0.4) X 10(4) and (2.6 +/- 0.1) X 10(5) M−1 for GlcNac, (GlcNac)2 and (GlcNac)3 respectively. The binding enthalpy, delta H0, for the three glucosaminides were very low and ranged from −12.1 to −20.6 kJ X mol-1. The results are compared with those obtained with wheat-germ agglutinin, another GlcNac-specific gramineaous lectin.


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