title: A rapid purification procedure for pyruvate kinase from the hyphal fungus Aspergillus nidulans.
abstract: Pyruvate kinase was purified from the filamentous fungus Aspergillus nidulans with a 45-55% yield. The procedure involved dye-affinity chromatography and fast protein liquid chromatography, resulting in highly active and pure enzyme in milligram quantities within 2 days. The purified enzyme, a tetramer with a subunit molecular weight of 65,000 and an isoelectric point of 4.7, was used to determine the amino acid composition.
authors.affiliation: Department of Genetics, Agricultural University, Wageningen, The Netherlands.
authors.forename: H C
authors.initials: HC
authors.lastname: Kester
authors.forename: J H
authors.initials: JH
authors.lastname: Uitzetter
authors.forename: L H
authors.initials: LH
authors.lastname: de Graaff
authors.forename: J
authors.initials: J
authors.lastname: Visser
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001233:Aspergillus nidulans / Q000201:enzymology*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002846:Chromatography, Affinity / Q000379:methods; D004396:Coloring Agents; D011770:Pyruvate Kinase / Q000302:isolation & purification*
chemical_list: D000596:Amino Acids; D004396:Coloring Agents; D011770:Pyruvate Kinase