Localization and characterization of the carbohydrate-binding site of the porcine lymphocyte mannan-binding protein.
Mol Immunol
; 29(12): 1437-46, 1992 Dec.
Article
em En
| MEDLINE
| ID: mdl-1454063
ABSTRACT
Mannan-binding proteins found in the liver and serum of several vertebrate species are supposed to play an important role in the intracellular transport of glycoproteins, as well as in several protective reactions including complement activation and elimination of various pathogens. To study these protective functions at molecular level it is necessary to understand the fine oligosaccharide specificity and mutual relation among various forms of these soluble lectins. We have isolated mannan-binding protein as peripheral membrane proteins of porcine lymphocytes. This lectin was purified to homogeneity and shown to possess many properties in common with the well studied rat liver proteins (mol. mass, subunit composition and general organization of the molecule). Binding studies performed with three series of defined oligosaccharides (high mannose, hybrid type, and complex) on native lectin molecules as well as isolated carbohydrate-binding domains revealed distinctive features of this mannan-binding protein, including its impaired ability to bind the oligosaccharide ligand after reduction and decyclization at core N-acetyl-D-glucosamine 1.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Linfócitos
/
Proteínas de Transporte
/
Metabolismo dos Carboidratos
Limite:
Animals
Idioma:
En
Ano de publicação:
1992
Tipo de documento:
Article