Molecular mechanism by which cyclic amp regulates myocardial contractility Page: 63 of 153
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38
TABLE I
Effect of trypsin on phosphorylated and nonphosphorylated
microsomes. In the top half of the table, microsomes were
phosphorylated for 10 min as described in "Methods". Trypsin was
then added at various concentrations ranging from 0.1 mg/ml to 0.5
mg/ml. After an additional 10 min, the reaction was stopped by
adding Laemmli solubilizing buffer. The samples were
electrophoresed on a 12% polyacryl ami de-SDS-sl ab gel,
autoradiographed, and the amount of radioactivity in each band was
compared with the control, which had not been subjected to
trypsin. In the bottom half of the table, microsomes were first
treated with trypsin for 10 min at 25°, then trypsin inhibitor
was added at a trypsin inhibitor to trypsin ratio of 2:1. At this
point, cyclic AMP, protein kinase and [y - ^P]ATP were
added. After an additional 10 min, the reaction was stopped with
Laemml i sol ubi 1 izi ng buffer.
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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/m1/63/: accessed July 17, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; crediting UNT Libraries Government Documents Department.