Cyclic nucleotide-dependent protein kinases. IX. Partial purification and some properties of guanosine 3',5'-monophosphate-dependent and adenosine 3',5'-monophosphate-dependent protein kinases from various tissues and species of Arthropoda.

The distribution of protein kinases activated specifically by low concentrations of guanosine 3’,5’-monophosphate (cyclic GMP) or adenosine 3’,5’-monophosphate (cyclic AMP) in various tissues and species of Arthropoda was studied. The Arthropoda were found to represent a rich source of cyclic GMP-dependent protein kinases. The relative levels of cyclic GMP-dependent and cyclic AMP-dependent protein kinases varied widely among different tissues of a species and among similar tissues of different species. The proportions found ranged from apparently all cyclic GMP-dependent enzyme (in silkmoth fat body) to apparently all cyclic AMP-dependent enzyme (in lobster gill), other tissues exhibiting various intermediate ratios. Evidence was obtained of dissimilarities between these two classes of protein kinase and between the cyclic AMP-dependent protein kinases of arthropod and of mammalian origin, including specificity for protein substrates and pattern of activation by divalent cations. Interestingly, the cyclic GMPdependent protein kinases of arthropods and the cyclic AMP-dependent protein kinases of vertebrates tended to resemble one another in these respects. Within each class of enzyme, preparations from different tissues also varied significantly in their characteristics. The variable ratios of cyclic GMP-dependent and cyclic AMP-dependent protein kinases in tissues, coupled with their different characteristics, suggest that cyclic GMP and cyclic AMP are specific and distinct from one another in terms of their biochemical and physiological actions.