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Purification and properties of pyruvate kinase type M1 from bovine brain.

作者信息

Terlecki G

机构信息

Department of Biochemistry, Medical School of Wrocław, Poland.

出版信息

Int J Biochem. 1989;21(9):1053-60. doi: 10.1016/0020-711x(89)90240-1.

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.
摘要

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