Abstract
cAMP-dependent protein kinase activity in the soluble fraction was decreased in both v-H-ras-transformed and activated-c-H-ras-transformed NIH3T3 cells as compared with that in NIH3T3 cells. Both of the elution profile of type II cAMP-dependent protein kinase from DEAE-cellulose and the electrophoretic behavior of its regulatory subunits in the particulate fraction of H-ras-transformed cells are different from those of control NIH3T3 cells. These results suggest that ras protein causes the alterations of some properties of cAMP-dependent protein kinases.
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