The binding site of chicken hepatic lectin.
نویسندگان
چکیده
منابع مشابه
The 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 ...
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...
متن کاملSelective 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 کاملLectin-Binding Patterns in the Microenvironment of the Mouse Developing T-Cells
Glycoconjugates and their programmed changes during the course of development in the cell-surface as well as in the extracellular matrix, are known to affect cell differentiation, cellular interaction and other developmental phenomena during embryogenesis. The purpose of this study was to localize N-acetylgalactosamin as well as fucose-containing glycoconjugates in situ during thymus developmen...
متن کاملBinding of the mannose-specific lectin, griffithsin, to HIV-1 gp120 exposes the CD4-binding site.
The glycans on HIV-1 gp120 play an important role in shielding neutralization-sensitive epitopes from antibody recognition. They also serve as targets for lectins that bind mannose-rich glycans. In this study, we investigated the interaction of the lectin griffithsin (GRFT) with HIV-1 gp120 and its effects on exposure of the CD4-binding site (CD4bs). We found that GRFT enhanced the binding of H...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1983
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)44207-4