Molecular mechanism by which cyclic amp regulates myocardial contractility Page: 90 of 153
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the 22,000 dalton protein is soluble in a low concentration of
deoxycholate. After phosphorylation, the protein cannot be
solubilized by deoxycholate. These results intimate that
phosphorylation causes the protein to become buried in the
membrane, rendering it resistant to agents acting on the exterior
of the membrane (Bidlack and Shamoo, 1979b).
The Ca2+ + Mg2+-ATPase, a 100,000 dalton protein, is the
integral protein of both cardiac and skeletal sarcoplasmic
reticulum. It actively transports calcium into the sarcoplasmic
reticulum. The ATPase from skeletal rabbit hind muscle was first
isolated almost a decade ago by MacLennan (1970). As a result, the
skeletal enzyme has been characterized much more extensively than
2+
the cardiac enzyme. In both systems, 2 moles of Ca are
transported for each mole of ATP hydrolyzed (Hasselbach, 1964;
Weber, 1966). The Ca2+ + Mg2+-ATPase from skeletal and cardiac
sarcoplasmic reticulum differ with respect to calcium binding,
uptake, Km for calcium and hydrolytic activity. They have
similar values for ATP (Shigekawa et al_., 1976). Recently two
2+
methods have been published for the isolation of the Ca +
Mg -ATPase from cardiac sarcoplasmic reticulum (Levitsky et al.,
1976; Van Winkle et_ al_., 1978). The method presented in this
communication has the advantage over these two procedures in that
it is a very rapid technique employing very low concentrations of
detergent. Moreover, our method also isolates for the first time
the 22,000 dalton protein from the cardiac sarcoplasmic reticulum.
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Bidlack, J. M. Molecular mechanism by which cyclic amp regulates myocardial contractility, report, January 1, 1979; United States. (https://digital.library.unt.edu/ark:/67531/metadc1085147/m1/90/: accessed July 17, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; crediting UNT Libraries Government Documents Department.