title: Enzymatic properties of pyruvate kinase from the rumen ciliates genus Entodinium.
abstract: 1. Pyruvate kinase from the rumen ciliates genus Entodinium was partially purified and the enzymatic properties were investigated. 2. Three types of pyruvate kinase (type I, II and III) on DEAE-cellulose column were eluted with a linear gradient of KCl. The enzymatic properties differed among the types of enzyme, especially type I and type III displayed different kinetic properties to each other. The enzymatic property of type II enzyme was an intermediate between type I and III. 3. The principal enzyme, type I, required a divalent cation, Mg2+ and was activated with AMP and FDP. ATP was a potent inhibitor. The saturation curves for the substrates, PEP and ADP, were hyperbolic and Km values were 0.15 and 0.27 mM, respectively.
authors.affiliation: Faculty of Bioresources, Mie University, Tsu, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Wakita
authors.forename: S
authors.initials: S
authors.lastname: Hoshino
mesh_terms: D000249:Adenosine Monophosphate / Q000502:physiology; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D016798:Ciliophora / Q000201:enzymology*; D005635:Fructosediphosphates / Q000502:physiology; D066298:In Vitro Techniques; D011770:Pyruvate Kinase / Q000378:metabolism*; D012417:Rumen / Q000469:parasitology*; D012756:Sheep / Q000469:parasitology
chemical_list: D005635:Fructosediphosphates; D000249:Adenosine Monophosphate; D011770:Pyruvate Kinase