Isolation of a novel plant lectin with an unusual specificity from Calystegia sepium |
| |
Authors: | Willy J Peumans Harry C Winter Veronique Bemer Fred Van Leuven Irwin J Goldstein Paolo Truffa-Bachi Els J.M Van Damme |
| |
Affiliation: | (1) Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Willem de Croylaan 42, 3001 Leuven, Belgium;(2) Department of Biological Chemistry, The University of Michigan, 1301 Catherine Road, Ann Arbor, MI 48109-0624, USA;(3) Unite d'Immunophysiologie Moleculaire, CNRS LA 1961, Departement d'Immunologie, Institut Pasteur, 25 Rue du Dr. Roux, 75724 Paris Cedex 15, France;(4) Centre for Human Genetics, Katholieke Universiteit Leuven, Herestraat 49, 3001 Leuven, Belgium |
| |
Abstract: | A novel plant lectin has been isolated from the rhizomes of Calystegia sepium (hedge bindweed) and partially characterized. The lectin is a dimeric protein composed of two identical non-covalently linked subunits of 16kDa. Hapten inhibition studies indicate that the novel lectin is best inhibited by maltose and mannose and hence exhibits a sugar binding specificity that differs in some respects from that of all previously isolated plant lectins. Mitogenicity tests have shown that the Calystegia lectin is a powerful T-cell mitogen. Affinity purification of human, plant and fungal glycoproteins on immobilized C. sepium lectin demonstrates that this novel lectin can be used for the isolation of glycoconjugates from various sources. Moreover, it can be expected that by virtue of its distinct specificity, the new lectin will become an important tool in glycobiology. Abbreviations: Calsepa, lectin isolated from Calystegia sepium; ConA, concanavalin A; LPS, lipopolysaccharide; PBS, phosphate buffered saline (1.5 mMKH2PO4, 10 mM Na2HPO4, 3 mM KCl, 140 mM NaCl, pH 7.4) This revised version was published online in November 2006 with corrections to the Cover Date. |
| |
Keywords: | Calystegia lectin maltose mannose |
本文献已被 SpringerLink 等数据库收录! |
|