Biomaterial Database

Structural requirements for the binding of oligosaccharides and glycopeptides to immobilized wheat germ agglutinin. 1981

K Yamamoto, and T Tsuji, and I Matsumoto, and T Osawa

The structural requirements for the interaction of asparagine-linked oligosaccharide moieties of glycoproteins with wheat germ agglutinin (WGA) were investigated by using affinity chromatography on a WGA-Sepharose column. So-called hybrid-type glycopeptides obtained from ovalbumin [Yamashita, K., Tachibana, Y., & Kobata, A. (1978) J. Biol. Chem. 253, 3862--3869] were found to have high affinity for WGA--Sepharose, whereas high mannose-type and complex-type glycopeptides were shown to have low affinity. The elution profiles of various glycopeptides modified by glycosidase treatment, Smith periodate degradation, acetolysis, and hydrazinolysis showed that the GlcNAcbeta 1--4Manbeta 1--4GlcNAc beta 1--4GlcNAc-Asn structure was essential for the binding of glycopeptides to a WGA-Sepharose column. Thus, it was revealed that both the N,N'-diacetylchitobiose moiety and the beta-N-acetylglucosaminyl residue linked to C-4 of the beta-linked mannose residue contributed to the interaction of the glycopeptide with WGA-Sepharose. The substitution at C-6 of the innermost beta-N-acetylglucosaminyl residue by an alpha-fucosyl residue or at C-6 of the beta-linked mannose residue by another mannose residue in the above structure reduced the affinity of glycopeptides for the column.

UI	MeSH Term	Description	Entries
D009844	Oligosaccharides	Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.	Oligosaccharide
D002846	Chromatography, Affinity	A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D006020	Glycopeptides	Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight.	Glycopeptide
D013329	Structure-Activity Relationship	The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.	Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships
D014909	Wheat Germ Agglutinins	Lectins purified from the germinating seeds of common wheat (Triticum vulgare); these bind to certain carbohydrate moieties on cell surface glycoproteins and are used to identify certain cell populations and inhibit or promote some immunological or physiological activities. There are at least two isoforms of this lectin.	Agglutinins, Wheat Germ,Lectins, Triticum Vulgare,Lectins, Wheat Germ,Triticum Vulgare Lectin,Triticum Vulgare Lectins,Wheat Germ Agglutinin,Wheat Germ Lectin,Wheat Germ Lectins,Wheat Germ Agglutinin Isolectin 1,Wheat Germ Agglutinin Isolectin 2,Agglutinin, Wheat Germ,Germ Agglutinin, Wheat,Germ Lectin, Wheat,Lectin, Triticum Vulgare,Lectin, Wheat Germ,Vulgare Lectin, Triticum
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