Protein kinase C, a protein related in PI cascade, was partially purfied from the cytosol protein of etiolated plant of Glycine max by DEAE-52 cellulose chromatography and phenylsepharose chromatography. When the DEAE column was eluted with 0-0.8 M linear gradient KCl, two fractions were found that increased the phosphorylation of histon H1 about five and nine-fold in the presence of 5 ㎛/mL phosphatidylserine and 0.5 ㎛/mL diolein, respectively. These fraction were used as DEAE pool. The fraction eluted with relatively high concentration of KCl was loaded on phenylsepharose column with 5 mM CaCl_2 and eluted with 1 mM EGTA. A fraction contained the protein kinase C, which increased the phosphorylation of the histon H1 was fractionated. To determine the molecular weight of PKC, the fraction eluted from Phenylsepharose column was analyzed by 5∼15% polyacrylamide gel electrophoresis after concentrated with the Amicon membrane (YM10). That revealed two bands corresponding to 60 and 65 kD by silver staining of the gel, respectively.