Improved purification and partial characterization of (Na+, K+)-ATPase from cardiac muscle |
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Authors: | Barry JR Pitts Arnold Schwartz |
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Institution: | Department of Cell Biophysics, Baylor College of Medicine, Houston, Texas 77025 U.S.A. |
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Abstract: | A method is described for purification of (N+, K+)-ATPase which yields approximately 60 mg of enzyme from 800 g of cardiac muscle with specific activities ranging from 340 to 400 μmol inorganic phosphate/mg protein per h (units/mg). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated the presence of a major 94 000 dalton polypeptide and four or five lesser components, one of which was a glycoprotein with an apparent molecular weight of 58 000. The enzyme preparation bound 600–700 pmol of 3H]ouabain/mg protein when incubated in the presence of either Mg2+ plus Pi or Mg2+ plus ATP plus Na+, and incorporated more than 600 pmol 32P/mg protein when incubated with γ-32P-labeled ATP in the presence of Mg2+ and Na+. The preparation is approximately 35% pure. |
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