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Ouabain‐ and Ca 2+ ‐sensitive ATPase activity of chimeric Na‐ and Ca‐pump molecules
Author(s) -
Luckie Douglas B.,
Boyd Kimberly L.,
Takeyasu Kunio
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80400-w
Subject(s) - ouabain , chemistry , atpase , diaphragm pump , ion pump , endoplasmic reticulum , biophysics , protein subunit , p type atpase , microbiology and biotechnology , biochemistry , ion , sodium , enzyme , biology , materials science , organic chemistry , micropump , nanotechnology , gene
Chimeric ion‐pumps, consisting of the N‐terminal of the α 1 ‐subunit of the ouabain‐sensitive chicken Na + , K + ‐ATPase and the C‐terminal of the sarcoplasmic reticulum Ca 2+ ‐ATPase, were expressed in ouabain‐insensitive mouse L cells. These chimeric molecules exhibited ouabain‐sensitive ATPase activity very similar to that of the wild‐type chicken Na + K + ‐ATPase. This ATPase activity could be stimulated by adding Ca 2+ to the assay system. These results suggest that the sites for ouabain‐inhibition are restricted to the N‐terminal of the Na‐pump, and the C‐terminal of the Ca‐pump interacts with Ca 3+ .