No abstract

No abstract

No abstract

When isolated intact rat liver mitochondria are incubated with [Y-~*P]ATP the major phosphoryfated proteins are those of 47 and 36 kDa. Phosphorylation of the 4'7 kDa protein, but not of the 36 kDa protein, is inhibited by ~arboxyatractyloside, an inhibitor of mitochondrial ATP uptake, while phosphorylation of the 36 kDa protein is inhibited by various uncouplers and an inhibitor of mitochondrial respiration. Addition of purified protein kinase C to the isolated mitochondria leads to the phasphorylation of 69, 37 and 17 kDa Proteins. As with other substrates for protein kinase C, phosphorylat~~~ of these proteins is dependent on Ca2+ and markedly stimulated by various tumor promoters.

No abstract