BIOMAT Database Logo BIOMAT Database Logo

An immunochemical study of the combining sites of the second lectin isolated from Bandeiraea simplicifolia (BS II). 1978

C Wood, and E A Kabat, and S Ebisu, and I J Goldstein

UI MeSH Term Description Entries
D007983 Lewis Blood Group Antigens Carbohydrate antigens structurally related to the ABH BLOOD-GROUP SYSTEM. They may occur as a modification of saccharide chains on glycolipids or glycoproteins on cell surfaces or in plasma, or as free oligosaccharides in secretions. Lewis antigens are not synthesized in blood cells. Instead Lewis glycolipids present in plasma are absorbed onto the surface of ERYTHROCYTES; LYMPHOCYTES; and PLATELETS. The phenotypes Le(a) and Le(b) are the result of the actions of two genes the Le gene (fucosyltransferase FUT3) and the Se gene (fucosyltransferase FUT2) on the precursor carbohydrate, glycolipid or glycoprotein. Other FUCOSYLTRANSFERASES can also synthesize the Lewis antigens. Blood Group Lewis Related Antigens,Lewis Antigen Related Tumor-Associated Antigens,Lewis Antigens,Lewis Blood Group Related Antigens,Lewis Blood Group Related Tumor-Associated Antigens,Lewis Blood-Group System,Lewis Related Antigens,Lewis System,Sialyl Lewis Antigens,Le Antigens,Le(a) Blood Group System,Antigens, Lewis,Antigens, Lewis Related,Antigens, Sialyl Lewis,Blood-Group System, Lewis,Lewis Antigen Related Tumor Associated Antigens,Lewis Blood Group Related Tumor Associated Antigens,Lewis Blood Group System
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
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
D011233 Precipitin Tests Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate. Precipitin Test,Test, Precipitin,Tests, Precipitin
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
D000017 ABO Blood-Group System The major human blood type system which depends on the presence or absence of two antigens A and B. Type O occurs when neither A nor B is present and AB when both are present. A and B are genetic factors that determine the presence of enzymes for the synthesis of certain glycoproteins mainly in the red cell membrane. ABH Blood Group,ABO Blood Group,ABO Factors,Blood Group H Type 1 Antigen,H Blood Group,H Blood Group System,ABO Blood Group System,Blood Group, ABH,Blood Group, ABO,Blood Group, H,Blood-Group System, ABO,Factors, ABO,System, ABO Blood-Group
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
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

Related Publications

C Wood, and E A Kabat, and S Ebisu, and I J Goldstein
Bandeiraea simplicifolia lectin II.
January 1978, Methods in enzymology,
C Wood, and E A Kabat, and S Ebisu, and I J Goldstein
BS II lectin: a second hemagglutinin isolated from Bandeiraea simplicifolia seeds with affinity for type III polyagglutinable red cells.
October 1977, Vox sanguinis,
C Wood, and E A Kabat, and S Ebisu, and I J Goldstein
Further characterization of the combining sites of Bandeiraea (Griffonia) simplicifolia lectin-I, isolectin A(4).
November 1999, Glycobiology,
C Wood, and E A Kabat, and S Ebisu, and I J Goldstein
Improved procedures for purification of the Bandeiraea simplicifolia I isolectins and Bandeiraea simplicifolia II lectin by affinity chromatography.
November 1980, European journal of biochemistry,
C Wood, and E A Kabat, and S Ebisu, and I J Goldstein
Serological studies on an alpha-D-galactosyl-binding lectin isolated from Bandeiraea simplicifolia seeds.
January 1976, Vox sanguinis,
C Wood, and E A Kabat, and S Ebisu, and I J Goldstein
An -N-acetyl-D-glycosamine binding lectin from Bandeiraea simplicifolia seeds.
November 1976, Archives of biochemistry and biophysics,
C Wood, and E A Kabat, and S Ebisu, and I J Goldstein
The use of 4-methylumbelliferyl glycosides in binding studies with the lectins BS I-A4, BS I-B4 and BS II from Bandeiraea (Griffonia) simplicifolia.
April 1981, FEBS letters,
C Wood, and E A Kabat, and S Ebisu, and I J Goldstein
A lectin-immunofluorometric assay using an immobilized Bandeiraea simplicifolia II lectin for the determination of galactosylation variants of glycoproteins.
March 1989, Analytical biochemistry,
C Wood, and E A Kabat, and S Ebisu, and I J Goldstein
Circular dichroism studies on the alpha-D-galactopyranosyl binding lectin isolated from the seeds of Bandeiraea simplicifolia.
January 1976, Biochemistry,
C Wood, and E A Kabat, and S Ebisu, and I J Goldstein
Distribution of Bandeiraea simplicifolia lectin binding sites in the genital organs of female and male mice.
January 1983, Histochemistry,
Copied contents to your clipboard!