title: Affinity chromatography of endoglucanase of Trichoderma viride by concanavalin A-agarose.
abstract: Endoglucanase (C kappa cellulase) and cellobiase are often cross-contaminated in separation procedures by ion-exchange chromatography such as DEAE-cellulose. By using concanavalian A (Con A)-agarose chromatography, C kappa cellulase and cellobiase from Trichoderma virde can be separated. C kappa cellulase showed affinity toward Con A. indicating a glycoprotein containing alpha-D-mannopyransyl and alpha-D-glucopyranosyl end groups or internal 2-O-D-mannopyranosyl residues in sugar moieties. This method provides a way to estimate the quantities of C kappa enzyme produced by T. viride and possibly by other organisms.
mesh_terms: D001665:Binding Sites; D002480:Cellulase / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity / Q000379:methods*; D003208:Concanavalin A; D003904:Mitosporic Fungi / Q000201:enzymology*; D011134:Polysaccharides; D012685:Sepharose; D014242:Trichoderma / Q000201:enzymology*; D001617:beta-Glucosidase / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D011134:Polysaccharides; D003208:Concanavalin A; D012685:Sepharose; D001617:beta-Glucosidase; D002480:Cellulase