1.
Biosci Biotechnol Biochem
; 73(1): 237-40, 2009 Jan.
Artigo
em Inglês
| MEDLINE
| ID: mdl-19129647
RESUMO
Human macrophage dectin-1, a type II transmembrane beta-glucan receptor, was expressed as a fusion protein with an N-terminal hexahistidine tag and glutathione S-transferase in an Escherichia coli cell-free translation system, and assayed for binding specificity. Recombinant dectin-1 specifically bound to some beta-glucans, but not to other carbohydrates. The beta-glucan binding of recombinant dectin-1 was inhibited by laminarin, a soluble beta-glucan, and by laminarioligosaccharides, but not by other carbohydrates. These results suggest that recombinant human dectin-1 can be used as a useful probe in identifying ligands in humans and tonic foods due to its strict binding specificity.