title: The lanthanide-enhanced affinity chromatography of clostridial collagenase.
abstract: Clostridiopeptidase A (EC 3.4.24.3) did not bind to a collagen affinity column in the absence of Ca2+, but did so in the presence of lanthanide ions (Ln3+). The sequestered enzyme could be eluted with EGTA. For the four Ln3+ ions tested, the order of efficiency in promoting enzyme binding, Sm3+ greater than Lu3+ greater than Er3+ much greater than La3+, reflected their relative abilities to inhibit clostridiopeptidase A. By using Sm3+ as an adjunct, it proved possible to separate a highly active preparation of collagenase from crude clostridial collagenase. Sodium dodecyl sulphate/polyacrylamide-gel-electrophoretic analysis of the preparation revealed a major protein of Mr 95000 and a minor component of Mr 82000. As both were stained by periodic acid/Schiff reagent, they were probably glycoproteins.
authors.forename: C H
authors.initials: CH
authors.lastname: Evans
mesh_terms: D002846:Chromatography, Affinity / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D008674:Metals, Rare Earth; D003012:Microbial Collagenase / Q000302:isolation & purification*
chemical_list: D008674:Metals, Rare Earth; D003012:Microbial Collagenase