منابع مشابه
Endogenous lectins from cultured cells: subcellular localization of carbohydrate-binding protein 35 in 3T3 fibroblasts
In previous studies, a lectin designated as carbohydrate-binding protein 35 (CBP35) has been isolated from cultured 3T3 fibroblasts. In the present study, rabbit antibodies directed against CBP35 were used to analyze the subcellular distribution of CBP35 in 3T3 cells. Several lines of evidence indicate that CBP35 is found externally exposed at the cell surface: immunofluorescent staining of liv...
متن کاملInvolvement of water in carbohydrate-protein binding.
The interactions of trimannosides 1 and 2 with Con A were studied to reveal the effects of displacement of well-ordered water molecules on the thermodynamic parameters of protein-ligand complexation. Trisaccharide 2 is a derivative of 1, in which the hydroxyl at C-2 of the central mannose unit is replaced by a hydroxyethyl moiety. Upon binding, this moiety displaces a conserved water molecule p...
متن کاملEvidence that family 35 carbohydrate binding modules display conserved specificity but divergent function.
Enzymes that hydrolyze complex carbohydrates play important roles in numerous biological processes that result in the maintenance of marine and terrestrial life. These enzymes often contain noncatalytic carbohydrate binding modules (CBMs) that have important substrate-targeting functions. In general, there is a tight correlation between the ligands recognized by bacterial CBMs and the substrate...
متن کاملDevelopmentally regulated, carbohydrate-binding protein in Dictyostelium discoideum.
A carbohydrate-binding protein assayed by its ability to agglutinate formalinized sheep erythrocytes is synthesized between 3 and 9 hr after Dictyostelium discoideum cells are deprived of food, as the cells become cohesive. Agglutination of erythrocytes by this protein was inhibited by N-acetyl-D-galactosamine, D-galactose, and L-fucose, but other monosaccharides had little or no effect. The pr...
متن کاملLigand-mediated dimerization of a carbohydrate-binding molecule reveals a novel mechanism for protein-carbohydrate recognition.
The structural and thermodynamic basis for carbohydrate-protein recognition is of considerable importance. NCP-1, which is a component of the Piromyces equi cellulase/hemicellulase complex, presents a provocative model for analyzing how structural and mutational changes can influence the ligand specificity of carbohydrate-binding proteins. NCP-1 contains two "family 29" carbohydrate-binding mod...
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ژورنال
عنوان ژورنال: Trends in Glycoscience and Glycotechnology
سال: 1992
ISSN: 0915-7352,1883-2113
DOI: 10.4052/tigg.4.43