[Phosphorylation of cardiac sarcolemma proteins in isadrine myocarditis].
The incorporation of 33P into 54, 43 and 23 kDalton proteins of rabbit cardiac sarcolemma is demonstrated both in intact muscle and under isadrine myocarditis. The phosphorylation by cAMP-dependent protein kinase is shown only for the 23.5 kDalton protein. The level of this protein phosphorylation decreases under isadrine myocarditis in the presence of 10(-6) M cAMP and absence of "exogenic" protein kinase. In the preparations of the sarcolemma of the cardiac muscle under myocarditis the phosphorylation of the 23.5 kDalton protein is not stimulated by beta-agonists in the medium without "exogenic" protein kinase and cAMP. The latter being present, the phosphorylation reaches the control values.
D000818:Animals; D000242:Cyclic AMP / Q000378:metabolism; D066298:In Vitro Techniques; D007545:Isoproterenol / Q000494:pharmacology / Q000633:toxicity; D009124:Muscle Proteins / Q000378:metabolism*; D009205:Myocarditis / Q000139:chemically induced / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism*; D010766:Phosphorylation; D047428:Protein Kinase Inhibitors; D011817:Rabbits; D012508:Sarcolemma / Q000378:metabolism*
D009124:Muscle Proteins; D047428:Protein Kinase Inhibitors; D000242:Cyclic AMP; D007545:Isoproterenol
Fosforilirovanie belkov sarkolemmy serdechnoĭ myshtsy pri izadrinovom miokardite.