Biomaterial Database

Identification of peanut agglutinin-binding glycoproteins on immature human thymocytes. 1986

A De Maio, and H Lis, and J M Gershoni, and N Sharon

Previous studies in our laboratory have shown that peanut agglutinin (PNA), a lectin specific for the disaccharide Gal beta 3GalNAc, binds to immature (cortical) thymocytes of mouse and man and not to the mature (medullary) cells. Using lectin overlay of protein blots and lectin-affinity chromatography, we have found that the major PNA-binding glycoproteins on total as well as on immature (PNA+) human thymocytes correspond to two bands of Mr 170,000 and 180,000. Another glycoprotein, of Mr 110,000, also binds PNA but to a lesser extent. All three glycoproteins contain sialic acid as demonstrated by cell surface labeling with NaIO4-NaB3H4, binding of wheat germ agglutinin, and reaction with alkaline phosphatase-hydrazide. After treatment with sialidase, binding of PNA to these glycoproteins is significantly enhanced.

UI	MeSH Term	Description	Entries
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
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
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D012794	Sialic Acids	A group of naturally occurring N-and O-acyl derivatives of the deoxyamino sugar neuraminic acid. They are ubiquitously distributed in many tissues.	N-Acetylneuraminic Acids,Acids, N-Acetylneuraminic,Acids, Sialic,N Acetylneuraminic Acids
D013601	T-Lymphocytes	Lymphocytes responsible for cell-mediated immunity. Two types have been identified - cytotoxic (T-LYMPHOCYTES, CYTOTOXIC) and helper T-lymphocytes (T-LYMPHOCYTES, HELPER-INDUCER). They are formed when lymphocytes circulate through the THYMUS GLAND and differentiate to thymocytes. When exposed to an antigen, they divide rapidly and produce large numbers of new T cells sensitized to that antigen.	T Cell,T Lymphocyte,T-Cells,Thymus-Dependent Lymphocytes,Cell, T,Cells, T,Lymphocyte, T,Lymphocyte, Thymus-Dependent,Lymphocytes, T,Lymphocytes, Thymus-Dependent,T Cells,T Lymphocytes,T-Cell,T-Lymphocyte,Thymus Dependent Lymphocytes,Thymus-Dependent Lymphocyte
D019158	N-Acetylneuraminic Acid	An N-acyl derivative of neuraminic acid. N-acetylneuraminic acid occurs in many polysaccharides, glycoproteins, and glycolipids in animals and bacteria. (From Dorland, 28th ed, p1518)	Sialic Acid,Acid, N-Acetylneuraminic,Acid, Sialic,N Acetylneuraminic Acid
D019887	Peanut Agglutinin	Lectin purified from peanuts (ARACHIS HYPOGAEA). It binds to poorly differentiated cells and terminally differentiated cells and is used in cell separation techniques.	Peanut Lectin,Agglutinin, Peanut,Lectin, Peanut
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