Selective binding of N-acetylglucosamine to the chicken hepatic lectin
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چکیده
منابع مشابه
Selective binding of N-acetylglucosamine to the chicken hepatic lectin.
Among Ca2+-dependent (C-type) animal lectins, the chicken hepatic lectin (CHL) is unique in displaying almost complete selectivity for N-acetylglucosamine over other monosaccharide ligands. The crystal structures of the carbohydrate-recognition domain (CRD) from serum mannose-binding protein (MBP) and of a complex between the CRD from liver MBP and the methyl glycoside of N-acetylglucosamine we...
متن کاملThe binding site of chicken hepatic lectin.
The binding site of the chicken hepatic lectin involved in the clearance of N-acetylglucosamine-terminated serum glycoproteins was explored by a competitive binding assay using 3H-labeled agalacto-orosomucoid and various glycoproteins, polysaccharides, monosaccharides, and glycosides as inhibitors. The binding site is relatively small, involving a terminal nonreducing DGlcNAc structure with an ...
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The binding of N-acetylglucosamine (NAG) to chicken egg lysozyme (E.C. 3.2.1.17) was investigated by high-resolution X-ray powder diffraction at room temperature. NAG was found to bind to lysozyme in a rapid precipitation preparation with 0.05 M NaCl buffer pH 6.0, but not 0.05 M NaCl buffer pH 5.0. Binding was indicated by significant and readily apparent changes in the diffraction pattern fro...
متن کاملThe chicken receptor for endocytosis of glycoproteins contains a cluster of N-acetylglucosamine-binding sites.
The oligomeric state of the chicken hepatic receptor for N-acetylglucosamine-terminated glycoproteins (the chicken hepatic lectin) has been examined in detergent solution, in various membrane preparations, and in hepatocytes. In detergent solution, the cross-linking reagent, 1,5-difluoro-2,4-dinitrobenzene produces covalent complexes containing up to six receptor polypeptides. This result, alon...
متن کاملThe binding site of rabbit hepatic lectin.
A hepatic lectin responsible for the clearance of desialylated serum glycoproteins was immobilized on Sepharose and the binding site was examined by a competitive binding assay using a 3H-labeled precursor blood group Ii glycoprotein and various glycoproteins, polysaccharides monosaccharides, and glycosides as inhibitors. The binding site is relatively small, involving a terminal sugar containi...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1997
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3240673