Molecular mechanism by which cyclic amp regulates myocardial contractility

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Description

From these experiments, it appears that the phosphorylated 22,000 dalton protein does not regulate the transport properties of the ATPase. Instead phosphorylation of the 22,000 dalton protein causes it to become buried in the membrane, transporting Ca/sup 2 +/ into the sarcoplasmic reticulum and thereby, elevating the Ca/sup 2 +/ concentration in the sarcoplasmic reticulum available for release to the myofibrils.

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Pages: 142

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Bidlack, J. M. January 1, 1979.

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Description

From these experiments, it appears that the phosphorylated 22,000 dalton protein does not regulate the transport properties of the ATPase. Instead phosphorylation of the 22,000 dalton protein causes it to become buried in the membrane, transporting Ca/sup 2 +/ into the sarcoplasmic reticulum and thereby, elevating the Ca/sup 2 +/ concentration in the sarcoplasmic reticulum available for release to the myofibrils.

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Pages: 142

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Dep. NTIS, PC A07/MF A01.

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  • Other Information: Thesis

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  • January 1, 1979

Added to The UNT Digital Library

  • Feb. 10, 2018, 10:06 p.m.

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  • May 19, 2021, 12:57 p.m.

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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/: accessed July 17, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; crediting UNT Libraries Government Documents Department.

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