Abstract
Publisher Summary Cyclic AMP (cAMP)-dependent protein kinases catalyze the transfer of the terminal phosphate of ATP to serine or threonine residues of a variety of protein substrates. These enzymes are termed cAMP-dependent becasue most if not all of their activity is revealed only in the presence of low concentrations of cAMP. The enzymes are composed of two subunit types, one of which is catalytically active (C) and another (R) which regulates the activity of the catalytic subunit. The subunit R inhibits the activity of C until cAMP is bound to R at which time the subunits dissociate and the activity of the enzyme is expressed. Currently, it appears that there is more than one cAMP dependent protein kinase present in muscle and liver. In most of the cases investigated, at least two peaks of cAMP-dependent activity can be separated by chromatography on DEAE-cellulose. These fractions will be referred to as peak I and peak II protein kinase in communication. To date, no clear-cut differences in the physiological roles of these enzyme forms have been demonstrated.
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