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O-linked neutral sugar chains of porcine zona pellucida glycoproteins. 1993

T Hirano, and S Takasaki, and J L Hedrick, and N J Wardrip, and J Amano, and A Kobata
Department of Biochemistry, University of Tokyo, Japan.

The O-linked sugar chains were liberated from porcine zona pellucida glycoproteins by alkaline-borohydride treatment and the structures of neutral oligosaccharides were determined. The major oligosaccharides had the following structures with type-1 cores, (Gal beta 1-->4GlcNAc beta 1-->3)1 3-Gal bdta 1-->3N-acetylgalactosaminitol (54%) and GlcNAc beta 1-->3(Gal beta 1-->4GlcNAc beta 1-->3)0-1Gal beta 1-->3N- acetylgalactosaminitol (16%). Approximately 6% of the oligosaccharides had the structure with a type-3 core, Gal beta 1-->4GlcNAc beta 1-->3N-acetylgalactosaminitol. Oligosaccharides having alpha-galactose (2%) and beta-GalNAc (4%) at their non-reducing termini were also found as minor components.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
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
D002240 Carbohydrate Sequence The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS. Carbohydrate Sequences,Sequence, Carbohydrate,Sequences, Carbohydrate
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
D006023 Glycoproteins Conjugated protein-carbohydrate compounds including MUCINS; mucoid, and AMYLOID glycoproteins. C-Glycosylated Proteins,Glycosylated Protein,Glycosylated Proteins,N-Glycosylated Proteins,O-Glycosylated Proteins,Glycoprotein,Neoglycoproteins,Protein, Glycosylated,Proteins, C-Glycosylated,Proteins, Glycosylated,Proteins, N-Glycosylated,Proteins, O-Glycosylated
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013552 Swine Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA). Phacochoerus,Pigs,Suidae,Warthogs,Wart Hogs,Hog, Wart,Hogs, Wart,Wart Hog
D015044 Zona Pellucida A tough transparent membrane surrounding the OVUM. It is penetrated by the sperm during FERTILIZATION.
D034781 Receptors, N-Acetylglucosamine Cell surface receptors that bind to ACETYLGLUCOSAMINE. N-Acetylglucosamine Receptors,GlcNAc Specific Lectin,N-Acetylglucosamine Receptor,N-Acetylglucosamine Specific Lectin,Receptor, N-Acetylglucosamine,Lectin, GlcNAc Specific,Lectin, N-Acetylglucosamine Specific,N Acetylglucosamine Receptor,N Acetylglucosamine Receptors,N Acetylglucosamine Specific Lectin,Receptors, N Acetylglucosamine
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

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