Interaction of rice (Oryza sativa) lectin with N-acetylglucosaminides. Fluorescence studies

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. Additio...

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Bibliographic Details
Published in:Biochemical journal 1985-08, Vol.229 (3), p.687-692
Main Authors: Tabary, F, Frenoy, J.P
Format: Article
Language:English
Subjects:
Acetylglucosamine - analogs & derivatives
Acetylglucosamine - metabolism
Binding Sites
fluorescence
Glucosamine - analogs & derivatives
Kinetics
Lectins
N-acetylglucosamine
Oryza
Oryza sativa
Plant Lectins
purification
Spectrometry, Fluorescence
Temperature
Thermodynamics
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Summary: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.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2290687