Cardiac Contractile Protein Phosphatases PURIFICATION OF TWO ENZYME FORMS AND THEIR CHARACTERIZATION WITH SUBUNIT-SPECIFIC ANTIBODIES

@inproceedings{C2001CardiacCP,
  title={Cardiac Contractile Protein Phosphatases PURIFICATION OF TWO ENZYME FORMS AND THEIR CHARACTERIZATION WITH SUBUNIT-SPECIFIC ANTIBODIES},
  author={C... and L.. and J.. and D.},
  year={2001}
}
Two forms of protein phosphatase which dephosphorylate cardiac myosin or myosin light chains and the inhibitory subunit of cardiac troponin were purified from bovine cardiac muscle. The enzymes were composed of subunits of M, = 63,000, 55,000, and 38,000 in a 1:l:l molar ratio (PT-1) or M, = 63,000 and 38,000 in a 1:l molar ratio (PT-2). Native gel electrophoresis and sucrose gradient sedimentation indicated that activity toward all three substrates was due to a single enzyme species. A… CONTINUE READING