1996 Volume 60 Issue 3 Pages 530-531
Two protein kinases, one from soybeans and the other from rice leaves, were partially purified by sequential chromagography. These protein kinases, which had molecular masses of 47 and 50 kDa, respectively, were found to be activated by calcium and phosphatidylserine and catalyze the phosphorylation of serine residue(s) of histone III-S.
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