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The (Ca2+-Mg2+)-ATPase from human erythrocyte membranes has been solubilized in Triton X-100 and purified on a calmodulin affinity chromatography column in the presence of phosphatidylserine, to limit the inactivation of the enzyme. The enzyme was purified at least 150 times when compared with the original ghosts and showed a specific activity of 3.8 mumol.mg-1.min-1. In sodium dodecyl sulfate-polyacrylamide gels, a single major band was visible at a position corresponding to a molecular weight of about 125,000; a minor band (11% of the total protein) was present at a position corresponding to Mr = 205,000. Upon incubation of the purified preparation with [32P]ATP, both bands were phosphorylated in proportion to their mass, suggesting that both were active forms of purified ATPase.
V Niggli, and
J T Penniston, and
E Carafoli
July 1981,
FEBS letters,
V Niggli, and
J T Penniston, and
E Carafoli
May 1980,
The Biochemical journal,
V Niggli, and
J T Penniston, and
E Carafoli
March 1981,
Endocrinology,
V Niggli, and
J T Penniston, and
E Carafoli
July 1980,
Biochimica et biophysica acta,
V Niggli, and
J T Penniston, and
E Carafoli
January 1988,
Advances in experimental medicine and biology,
V Niggli, and
J T Penniston, and
E Carafoli
December 1981,
Biochimica et biophysica acta,
V Niggli, and
J T Penniston, and
E Carafoli
December 1980,
Biochimica et biophysica acta,
V Niggli, and
J T Penniston, and
E Carafoli
January 1977,
Acta biologica et medica Germanica,
V Niggli, and
J T Penniston, and
E Carafoli
February 1978,
Archives of biochemistry and biophysics,
V Niggli, and
J T Penniston, and
E Carafoli
September 1984,
The Journal of biological chemistry,
