Molecular and Cellular Biochemistry

, Volume 6, Issue 3, pp 197–201 | Cite as

Pyruvate kinase from human skeletal muscle

  • Barbara Baranowska
  • Tadeusz Baranowski
Letters to the Editor


A simple method is described for the isolation of crystalline pyruvate kinase from human skeletal muscle. The enzyme was purified by ammonium sulfate fractionation, heat treatment and crystallization. Two crystal forms of pyruvate kinase differing in solubility but not in specific activity were found. The homogenous enzyme preparations in triethanolamine buffer, pH 7.6 reveal at 25° a specific activity of 245 U per mg protein, and of 340 U/mg in potassium phosphate buffer (50mm). The enzyme is activated by inorganic phosphate and fructosediphosphate to the same extent, and inhibited non competetively by ammonium ion. The molecular weight as measured by gel filtration is 220,000 daltons and the enzyme molecule is composed of 4 subunits.


Ammonium Pyruvate Heat Treatment Potassium Phosphate Buffer Ammonium Sulfate 
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Copyright information

© Dr. W. Junk b.v. Publishers 1975

Authors and Affiliations

  • Barbara Baranowska
    • 1
  • Tadeusz Baranowski
    • 1
  1. 1.Department of Biochemistry, Institute of Biochemistry and BiophysicsMedical Academy of WroclawPoland

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