Lectin from Bulbs of Crocus sativus Recognizing N-Linked Core Glycan: Isolation and Binding Studies Using Fluorescence Polarization

Abstract

Publisher Summary Crocus sativus lectin (CSL) is truly mannose specific—its binding is inhibited only by mannooligosaccharides and not by glucose or its oligomers or polymers. Other mannose-specific lectins are also isolated from bulbs of tulipa gesneriana , galanthus nivalis , narcissus pseudonarcissus , hippeastrum hybridum , and lycoris radiata . These mannose-binding lectins exhibit different binding specificities toward various yeast cells of different cell wall mannan structures, indicating that each lectin has its unique sugar-binding specificity. It was found that hen ovomucoid was a good inhibitor of CSL, but it did not inhibit other mannose-specific lectins from plant bulbs. The binding specificity of CSL was also analyzed, using various carbohydrates as ligand, by fluorescence polarization (FP), flow injection analysis, time-resolved fluorometry, and surface plasmon resonance; it was found that CSL specifically recognizes the N-glycan core pentasaccharide. This chapter focuses on the isolation of CSL from bulbs of crocus sativus and binding assay of CSL, using FP method.