The modification of (Na+ + K+) ATPase sensitivity to ouabain extraction of membrane constituents distinct from the enzyme

Lelievre, L.; Charlemagne, D.; Paraf, A.

Biochemical and Biophysical Research Communications 72(4): 1526-1533

1976


ISSN/ISBN: 0006-291X
PMID: 136964
DOI: 10.1016/s0006-291x(76)80187-8
Accession: 068521685

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Abstract
The (Na+ + K+)ATPase [EC 3.6.1.3] from mouse plasmocytoma MOPC 173 ascitic cells was resistant to ouabain in purified plasma membranes as 50% of the enzyme activity (E 1/2) was inhibited by 120 .mu.M ouabain. After 2 treatments by a sucrose-EDTA-imidazole buffer, the plasma membrane-bound enzyme recovered in the pellet was much more sensitive to ouabain inhibition (E 1/2 = 0.4 .mu.M). The original (Na+ + K+) ATPase sensitivity to ouabain can be restored by addition of concentrated supernatants from EDTA-treated membranes plus Ca2+ and Mg2+ to the pellet.