Abstract

The crude protein kinase modulator preparations obtained from several rat tissues (aorta, brain, heart, liver, lung, skeletal muscle, small intestine and testis) were separated into their stimulatory and inhibitory modulator components by Sephadex G-100 gel filtration. The isolated stimulatory modulator augmented the activity of guanosine 3′:5′-monophosphate-dependent protein kinase of both mammalian and arthropod origins; it had no effect, however, on the activity of adenosine 3′:5′-monophosphate-dependent protein kinase. The isolated inhibitory modulator, on the other hand, depressed the activity of cyclic AMP-dependent protein kinase; it was without effect on the activity of cyclic GMP-dependent protein kinase. The present findings indicate that in the mammal, apparently in contrast to the arthropoda, separate proteins are responsible for the stimulatory and the inhibitory activities of protein kinase modulator, and that the two classes of cyclic nucleotide-dependent protein kinases are regulated in an opposing manner by these two types of modulators.

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