[Isolation, purification and study of the properties of pyruvate kinase from the bovine adrenal cortex].
Pyruvate kinase (ATP: pyruvate 2-0-phosphotransferase, EC 2. 7. 1. 40) from bovine adrenal cortex was purified 243 fold. The whole purification procedure included ammonium sulphate fractionation, heat treatment, Sephadex HW-55 chromatography and phosphocellulose chromatography. The specific activity of the preparation is 15.6 U/mg at 30 degrees C, the yield--36%. Pyruvate kinase showed only one protein band as judged by sodium dodecyl sulphate acrylamide gel electrophoresis. The enzyme displayed a hyperbolic saturation curve with respect to P-enolpyruvate. The apparent Km for this substrate was 0.55 X 10(-4) M, pH optimum--6.8-7.0. K+ concentrations above 0.1 M inhibit the enzyme.
D000302:Adrenal Cortex / Q000201:enzymology*; D000818:Animals; D002417:Cattle; D002482:Cellulose / Q000031:analogs & derivatives; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003911:Dextrans; D004589:Electrophoresis, Disc; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D011188:Potassium / Q000494:pharmacology; D011770:Pyruvate Kinase / Q000302:isolation & purification*
D003911:Dextrans; D002482:Cellulose; C025614:sephadex; C008881:phosphocellulose; D011770:Pyruvate Kinase; D011188:Potassium
Vydelenie, ochistka i izuchenie svoĭstv piruvatkinazy iz kory nadpochechnikov byka.