Purification and properties of a protamine kinase from bovine kidney microsomes.

@article{Amick1992PurificationAP,
  title={Purification and properties of a protamine kinase from bovine kidney microsomes.},
  author={Grayson D. Amick and Smitha A. L. Narasimha Reddy and Zahi Damuni},
  journal={Archives of biochemistry and biophysics},
  year={1992},
  volume={297 1},
  pages={
          80-5
        }
}
About an eightfold increase in protamine kinase activity was detected following extraction of highly purified microsomes from bovine kidney with 1% Triton X-100. Relative to the soluble fraction, the microsomes contained about 30% protamine kinase activity. The microsomal protamine kinase was purified to apparent homogeneity. The purified enzyme exhibited an apparent M(r) approximately 45,000 as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by gel permeation… CONTINUE READING
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