Protein kinase activities in the parathyroid gland: proparathyroid hormone, parathyroid hormone and secretory protein-I as substrates for phosphorylation.

We have identified two protein kinase activities in homogenates of bovine parathyroid tissue following fractionation on DEAE columns. One of these is a protein kinase C based upon its requirement for calcium and phosphatidylserine and the other one is probably M kinase. The protein kinase C phosphorylated both proparathyroid hormone and parathyroid hormone but not secretory protein-I (SP-I). Neither N [1-34] or C [35-84] terminal hormonal fragments were phosphorylated, suggesting that the structure of the intact PTH molecule is required for recognition by the enzyme. A second kinase activity behaving like M kinase was also obtained. This activity, which was not separable from a cAMP dependent kinase, was maximal with only 50 mM MgCl2 as cofactor. SP-I was readily phosphorylated by this activity but parathyroid hormone was not.