Isolation of a novel plant lectin with an unusual specificity from Calystegia sepium

摘要: A novel plant lectin has been isolated from the rhizomes of Calystegia sepium (hedge bindweed) and partially characterized. The is a dimeric protein composed two identical non-covalently linked subunits 16kDa. Hapten inhibition studies indicate that best inhibited by maltose mannose hence exhibits sugar binding specificity differs in some respects all previously lectins. Mitogenicity tests have shown powerful T-cell mitogen. Affinity purification human, fungal glycoproteins on immobilized C. demonstrates this can be used for isolation glycoconjugates various sources. Moreover, it expected virtue its distinct specificity, new will become an important tool glycobiology. Abbreviations: Calsepa, sepium; ConA, concanavalin A; LPS, lipopolysaccharide; PBS, phosphate buffered saline (1.5 mMKH2PO4, 10 mM Na2HPO4, 3 KCl, 140 NaCl, pH 7.4)