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Kahn, C. , and Neville, D. , J. Biol. Chem. 249, 4127-4131 (1974). 68. Soil, A. , Kahn, C. , and Neville, D. , J. Biol. Chem. 250, 4702-4707 (1975). 69. Soil, A. , Kahn, C. , Neville, D. , J. Clin. Invest. 56, 769-780 (1975). 70. , and Shooter, E. , J. Biol. Chem. 249, 6668-6674 (1974). 71. , Brain Res. 85, 337-341 (1975). 72. , Frazier, W. , and Bradshaw, R. , J. Biol. Chem. 251, 1516-1523 (1976). 73. , Frazier, W. , and Bradshaw, R. , J. Biol. Chem. 251, 1524-1530 (1976). 74. , Angeletti, P.
The cAMP-dependent protein kinase purified from rabbit skeletal muscle and studied by Krebs and his colleagues (81, 82) fulfills the criteria for a Type I enzyme. The purified bovine cardiac muscle protein kinase is a Type II kinase (83, 84). Since both enzymes have been highly purified, it is possible to compare them as prototypes of their respective categories. Details of this comparison will be cited in the next section. Briefly, both enzymes bind 2 moles cAMP/mole and have similar molecular weights and subunit composi tions, although it may be significant that the cAMP-binding protein subunit of the skeletal muscle kinase has a lower molecular weight (49,000) (85) than the analogous subunit of the cardiac muscle kinase (MW 55,000) (86).
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