Comparison of adenosine 3':5'-monophosphate-dependent protein kinases from rabbit skeletal and bovine heart muscle.

摘要: Homogeneous preparations of adenosine 3':5'-monophosphate (cyclic AMP)-dependent protein kinase from rabbit skeletal (Peak I) and bovine heart muscle have been compared. Each enzyme has an S20,w value 7.0. binds 2 mol cyclic AMP per is dissociated in the presence saturating concentrations into a demeric regulatory subunit-cyclic complex two catalytic subunits. The isolated subunits recombine, resulting formation original holoenzyme each case. Several differences between enzymes were found. Different salt are necessary for elution respective DEAE-cellulose. Their differ with respect to their sedimentation constants mobility on sodium dodecyl sulfate gel electrophoresis. subunit rapidly phosphorylated by MgATP but this does not occur enzyme. bound high affinity only different apparent dissociation Hill coefficients binding. With increases about 10-fold decreases coefficient, while phosphorylation cissociation constant 5- 6-fold coefficient. required dissociate enzymes. concentration