title: Purification and properties of pyruvate kinase type M1 from bovine brain.
abstract: 1. Pyruvate kinase type M1 was purified from bovine brain about 241-fold with 38% yield. 2. Specific activity of the enzyme was above 217 U/mg of protein (25 degrees C), relative mol. wt of the subunit--57,000 (+/- 2000) and pH optimum--6.8-7.2. 3. The enzyme shoved hyperbolic kinetics with Km value for PEP of 0.04 mM and for ADP of 0.3 mM. 4. Inorganic phosphate and ATP at concentrations below 4 mM showed activating effect, 1-phenylalanine and ATP above 6 mM--an inhibiting effect on the enzyme. 5. Inhibition by 1-phenylalanine was prevented by fructose-1,6-bisphosphate.
authors.affiliation: Department of Biochemistry, Medical School of Wrocław, Poland.
authors.forename: G
authors.initials: G
authors.lastname: Terlecki
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D002845:Chromatography / Q000379:methods; D004588:Electrophoresis, Cellulose Acetate; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification*; D007700:Kinetics; D011770:Pyruvate Kinase / Q000302:isolation & purification*
chemical_list: D007527:Isoenzymes; D011770:Pyruvate Kinase