Phosphorylation of endogenous proteins in response to calcium and calmodulin was assessed in membrane and cytosol from primate kidney. 2. Quantitative studies showed that calcium and calmodulin had little effect on phosphorylation in baboon kidney cytosol; in membranes, phosphorylation was significantly decreased by calcium and calmodulin. 3. Phosphorylation of specific proteins which had been electrophoretically separated indicated that calmodulin, in the absence or presence of calcium, enhanced bands of masses 37.1 +/- 1.1 kDa and 103.3 +/- 6.2 kDa (N = 6) in cytosol fractions of baboon kidney; in membrane fractions no effect was noted. 4. Similar results were found in normal human kidney.