The phosphorylation of several proteins in isolated nuclei from Pisum sativum L. was stimulated by spermine. Although spermine increased the general protein phosphorylation by 10 to 20%, it increased the phosphorylation of a 47 kilodalton polypeptide by 150%. By comparison other polyamines, spermidine, putrescine, and cadavarine had far less effect on the phosphorylation of the 47 kilodalton or any other polypeptide. Sodium fluoride was able to inhibit the phosphorylation of the 47 kilodalton polypeptide in the control, implying the participation of protein phosphatase(s) in the phosphorylation of nuclear proteins. Spermine stimulated the phosphorylation of the 47 kilodalton polypeptide over the controls, even in the presence of NaF. This result indicates that spermine probably activates a nuclear kinase, a conclusion supported also by thiophosphorylation data. The inability of ethyleneglycol-bis (beta-amino-ethyl ether)-N, N'-tetraacetic acid and Compound 48/80, a calmodulin antagonist, to inhibit this spermine stimulated phosphorylation renders improbable any role of calcium and calmodulin in mediating this response.