Dissociation and concomitant activation of adenosine 3′,5′-monophosphate-dependent protein kinase by histone

Abstract

Adenosine 3′,5′-monophosphate-dependent (cAMP-dependent) protein kinase from bovine brain has been examined after sedimentation in a sucrose density gradient. The molecular weight of the catalytic and of the cAMP binding protein decreased in the presence of low concentrations of either histone or cAMP, indicating that the enzyme had dissociated into subunits. The dissociation in the presence of histone was accompanied by conversion of the enzyme activity from a cAMP-dependent to a cAMP-independent form.