Biomaterial Database

Interaction of rice (Oryza sativa) lectin with N-acetylglucosaminides. Fluorescence studies. 1985

F Tabary, and 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.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D005944	Glucosamine		2-Amino-2-Deoxyglucose,Dona,Dona S,Glucosamine Sulfate,Hespercorbin,Xicil,2 Amino 2 Deoxyglucose,Sulfate, Glucosamine
D000117	Acetylglucosamine	The N-acetyl derivative of glucosamine.	Acetyl Glucosamine,N-Acetyl Glucosamine,N-Acetyl-beta-D-Glucosamine,N-Acetylglucosamine,beta-N-Acetylglucosamine,2-Acetamido-2-Deoxy-D-Glucose,2-Acetamido-2-Deoxyglucose,N-Acetyl-D-Glucosamine,2 Acetamido 2 Deoxy D Glucose,2 Acetamido 2 Deoxyglucose,Glucosamine, Acetyl,Glucosamine, N-Acetyl,N Acetyl D Glucosamine,N Acetyl Glucosamine,N Acetyl beta D Glucosamine,N Acetylglucosamine,beta N Acetylglucosamine
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D012275	Oryza	A genus of grass family (Poaceae) that include several rice species.	Oryza sativa,Rice,Rices
D013050	Spectrometry, Fluorescence	Measurement of the intensity and quality of fluorescence.	Fluorescence Spectrophotometry,Fluorescence Spectroscopy,Spectrofluorometry,Fluorescence Spectrometry,Spectrophotometry, Fluorescence,Spectroscopy, Fluorescence
D013696	Temperature	The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.	Temperatures
D013816	Thermodynamics	A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)	Thermodynamic
D037102	Lectins	Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.	Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal
D037121	Plant Lectins	Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.	Lectins, Plant,Phytagglutinin,Plant Agglutinin,Plant Lectin,Agglutinins, Plant,Phytagglutinins,Plant Agglutinins,Agglutinin, Plant,Lectin, Plant