Abstract
1. 1. Phosphorylation of rat liver endogenous substrates by protein kinase C (type III) was compared between cytosolic and paniculate (mitochondria, microsomes and plasma membrane) fractions. 2. 2. The rate and the maximum level of protein phosphorylation were several-fold higher in particulate fractions than in cytosolic fraction. 3. 3. Protein phosphorylation in cytosolic fraction was dependent on both Ca 2+ and phospholipid, but only Ca 2+ was necessary in phosphorylation of particulate fractions. 4. 4. These results suggest that protein kinase C (type III) has much more target proteins in particulate fractions rather than in cytosolic fraction and Ca 2+ was important regulator in particulate protein phosphorylation.
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