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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

Summary

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.

Keywords

Ammonium Pyruvate Heat Treatment Potassium Phosphate Buffer Ammonium Sulfate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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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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