Purification and properties of pyruvate kinase from Bacillus stearothermophilus.

@article{Sakai1986PurificationAP,
  title={Purification and properties of pyruvate kinase from Bacillus stearothermophilus.},
  author={Hideaki Sakai and Kiyoshi Suzuki and Kazutomo Imahori},
  journal={Journal of biochemistry},
  year={1986},
  volume={99 4},
  pages={1157-67}
}
Pyruvate kinase was purified to homogeneity from a moderate thermophile, Bacillus stearothermophilus. The molecular weight of the enzyme was found to be 250,000 on gel filtration and 242,000 on sedimentation analysis. The enzyme consisted of four identical subunits of a molecular weight of 62,000-64,000. There were no remarkable differences between the… CONTINUE READING