Purification and characterization of receptors for activated protein kinase C from rat hepatocytes.

It has been proposed that protein kinase C may be targeted to specific locations via interactions with anchoring proteins located at various subcellular sites. A group of proteins collectively termed RACKs (Receptors for Activated C-Kinase) have been identified. Here, we made use of a rapid and simple method to purify several RACKs from rat hepatocytes, taking advantage of the ability of these proteins to be precipitated with Triton X-100. The method can be used for the isolation of other proteins that share these properties. Four proteins were purified to apparent homogeneity with M(r) values of 14, 15, 16, and 34 kDa. Amino acid composition and biochemical characteristics of these proteins are presented.