Purification and kinetic properties of protein kinase C from cultured smooth muscle cells

Protein kinase C has been purified from in vitro cultures of A7r5 vascular smooth muscle cells. Three substrates have been employed for the kinetic analysis of the enzyme, Histone III-S, FKKSFKL-NH2 (analogous of the pseudo-substrate of the enzyme) and MBP4-14 (part of basic myelin protein) protein. The enzyme activity depends not only on the PKC-specific sequence motif, common to the three substrates, but also on additional structural motifs, which may be important also in governing the substrate selectivity of the enzyme in vivo.