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Correlation with stimulation of Ca2 -ATPase activity. J . Biol. Chem. 252, 3315-3323. Jones, L. , Phan, S. , and Besch, H. R . , Jr. (1978). Gel electrophoretic and density gradient analysis of the ( K + + Ca2+)-ATPase and the (Na+ t K+)-ATPase activities of cardiac membrane vesicles. Biochim. Biophys. Actu 514, 294-309. Jones, L. , Besch, H. , Flemming, J. , McConnaughey, M. , and Watanabe, A. M. (1979). Separation of vesicles of cardiac sarcolemma from vesicles of cardiac sarcoplasmic reticulum.
1983). The radioactively labeled’P-adrenergic antagonists that are commonly used to measure P-adrenergic receptors, such as [3H]dihydroalprenolo1described previously, are relatively nonselective in that they bind to PI- and p,-adrenergic receptors with approximately equal affinity. , 1983). , 1981). , 1983). Although the percentage of P,-adrenergic receptors in mammalian myocardium is small, they may be relevant clinically. , 1983). B. , 21 SARCOLEMMAL ENZYMES (1983a) covalently labeled P-adrenergic receptors in purified cardiac sarcolemma1 vesicles with this probe and then performed SDS-polyacrylamide gel electrophoresis and autoradiography to determine their molecular weights (Fig.
Photoincorporation of 8-N3-(32P]cAMP into type I1 regulatory subunits of different cardiac membrane fractions can be used to define the subcellular localization of particulate CAMP-dependent protein kinase activity in heart (Table 111). Type I1 regulatory subunits are highly concentrated in purified sarcolemmal vesicles, being almost completely absent from purified junctional and free cardiac sarcoplasmic reticulum vesicles. Indeed, the small levels of CAMP incorporation detected in the cardiac sarcoplasmic reticulum subfractions (58%) are easily explained by low levels of sarcolemmal contamination, as evidenced by the constant ratio of Na ,K -ATPase activity to cAMP photoincorporation in all of the subfractions examined (Table 111).