Abstract
We have examined the effects of a heat stable inhibitor protein on rat myocardial protein kinases obtained from nuclei, cytosol and a microsomal fraction. The inhibitor had no effect on protein kinases of the nuclear non-histone proteins. The protein kinases which precipitated at pH 4.8 from the cytosol were not inhibited by the inhibitor protein but the cAMP dependent protein kinases which remained in solution at pH 4.8 were inhibited. When histone was used as a substrate for the microsomal protein kinases the inhibitor protein inhibited the enzyme activity. In the presence of protamine as a substrate the protein kinase activity was not inhibited in the absence of cAMP but inhibited in the presence of cAMP. The effects of the inhibitor protein confirm that both cAMP dependent and cAMP independent protein kinases are found in the myocardial cell. The heat stable inhibitor protein may have an important role in cellular control.
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