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Title: Carbohydrate binding specificity of recombinant human macrophage beta-glucan receptor dectin-1. Author: Ujita M, Nagayama H, Kanie S, Koike S, Ikeyama Y, Ozaki T, Okumura H. Journal: Biosci Biotechnol Biochem; 2009 Jan; 73(1):237-40. PubMed ID: 19129647. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]