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• W2069852018 abstract "Treatment by EDTA of purified plasma membranes from MF2S cells (a variant of the murine plasmacytoma MOPC 173) solubilized proteins and increased by a 1000-fold the sensitivity of (Na+ + K+)-ATPase to ouabain. When added back with Ca2+ to treated plasma membranes, these EDTA-solubilized proteins restored the initial sensitivity of the enzyme to its inhibitor. We report the purification of a protein of Mr 32000, isolated from the EDTA-treated membrane supernatant. This protein was purified by a one-step procedure involving a preparative polyacrylamide gel electrophoresis without detergent. In the presence of Ca2+ it was able to restore the original sensitivity to ouabain of (Na+ + K+)-ATPase from EDTA-treated membrane. This protein was shown to be similar to the beta-actinin described by Maruyama by the following criteria: (1) molecular weight and amino acid composition; (2) cross-reactivity with their respective antisera; (3) in the presence of Ca2+ the same quantitative biological activity on ouabain sensitivity of the (Na+ + K+)-ATPase. A possible interaction between beta-actinin, calmodulin and membrane-bound (Na+ + K+)-ATPase is discussed." @default.
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• W2069852018 date "1982-11-01" @default.
• W2069852018 modified "2023-09-27" @default.
• W2069852018 title "Characterization of a β-actinin-like protein in purified non-muscle cell membranes. Its activity on (Na+ + K+)-ATPase" @default.
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• W2069852018 doi "https://doi.org/10.1016/0005-2736(82)90383-2" @default.
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