title: Purification of isocitrate lyase from Escherichia coli and watermelon using fast protein liquid chromatography.
abstract: The enzyme isocitrate lyase has been purified to gel electrophoretic homogeneity from Escherichia coli and watermelon. From cotyledons of the latter source, the enzyme is obtained in less than 8 hours after precipitation with (NH4)2 SO4 followed by fractionation on cationic Mono S microbeads and anionic Mono Q microbeads using Fast Protein Liquid Chromatography (FPLC). From a genetically engineered E. coli strain, in which high-level expression of isocitrate lyase occurs, the enzyme has been purified in one step from the high-speed supernatant using a Mono Q column with FPLC. These purifications, both of which give satisfactory yields, potentiate rapid access to isocitrate lyase from both prokaryotic and eukaryotic sources.
authors.affiliation: Biochemistry/Biophysics Program, Washington State University, Pullman 99164-4660.
authors.forename: M J
authors.initials: MJ
authors.lastname: Conder
authors.forename: Y H
authors.initials: YH
authors.lastname: Ko
authors.forename: B A
authors.initials: BA
authors.lastname: McFadden
mesh_terms: D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D005638:Fruit; D007522:Isocitrate Lyase / Q000302:isolation & purification*; D007652:Oxo-Acid-Lyases / Q000302:isolation & purification*; D010944:Plants / Q000201:enzymology*
chemical_list: D007652:Oxo-Acid-Lyases; D007522:Isocitrate Lyase