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Biomedical subjects

B F Korovkin

Publications and source records attributed to B F Korovkin.

At least 37 records · Page 2Linked to original sources
PubMed1981

[cAMP-dependent phosphorylation of myocardial troponin in experimental myocardial infarction].

cAMP-dependent phosphorylation of troponin, content of cAMP and the rate of the protein kinase complex activation were studied in dog heart muscle under conditions of experimental myocardial infarction. Incorporation of 32P into troponin I as well as the content of the cyclic nucleotide were shown to decrease in the impaired muscles as compared with the normal heart muscle. In experimental myocardial infarction the rate of the protein kinase complex dissociation appears to be altered as suggested by the fact that adrenaline stimulated dissimilarly the activity of cAMP-dependent protein kinase in vitro in presence and in absence of cAMP both in the intact and necrotized muscles.

Animals↗
PubMed1979

[Peculiarities of phosphorylation of skeletal muscle troponin under some forms muscle pathologies].

Phosphorylation of rat and rabbit troponin from normal skeletal muscles and from skeletal muscles of animals under avitaminosis, denervation and hypokinesia was studied. Phosphorylation was carried out by cAMP-dependent protein kinase with [gamma-33P] as substrate. The incorporation of labelled phosphorus into troponin T of the damaged muscles was decreased as compared to normal. After preliminary dephosphorylation of troponin by alkaline phosphatase immobilized on Sepharose 4B, the ability of damaged muscle troponin for subsequent phosphorylation was also decreased as compared to the control. It may be thus assumed that there exist conformational changes of troponin under muscular system pathologies.

Alkaline Phosphatase↗
PubMed1976

[Possible participation of cyclic AMP in regulating acid hydrolase activity in muscle tissue in avitaminosis E and denervation].

In the muscles of denervated and vitamin E-deficient rabbits the level of 3', 5'-cyclic AMP proved to decrease with a simultaneous increase in the activity of cAMP phosphodiesterase. In vivo experiments showed that at the concentration of 10(-4) cAMP was capable of retarding the release of acid phosphatase from the lysosome-rich fraction obtained from the muscles of E-deficient rabbits. Thus, in muscular dystrophy elevation of acid hydrolase activity in the skeletal muscle was due to leakage of the enzymes from the lysosomes as a result of decreased lysosome membrane stability because of decreased cAMP level.

3',5'-Cyclic-AMP Phosphodiesterases↗