Abstract
Publisher Summary This chapter discusses the catalytic subunit of cAMP-dependent protein kinase. The cAMP-dependent protein kinase has been shown to phosphorylate several proteins: (1) some enzymes, such as glycogen synthase and phosphorylase kinase, can be phosphorylated in more than one site and by more than one kinase (2) highly purified preparations of the cAMP dependent protein kinase are particularly useful in studies on proteins, which are phosphorylated at multiple sites or by multiple kinases. Preparations of the catalytic subunit of the cAMP-dependent protein kinase are used frequently because the catalytic subunit is easy to prepare and because the regulatory subunit has no known influence on catalytic activity when the concentration of cAMP is optimal. Preparation of the catalytic subunit involves dissociation of the subunits in the presence of cAMP. The tissue of choice appears to be the beef heart as it is available in large quantity, it contains predominantly type II protein kinase, and larger amounts of tissue extract can be adsorbed to a given amount of diethylaminoethyl (DEAE)-cellulose without overloading. The purification procedure can be scaled down by a factor of approximately 40 if only small amounts of C are needed.
Published Version
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