[Immunochemical properties of the regulatory subunit of cAMP-dependent protein kinase II].
Immunochemical analysis of the cAMP-dependent protein kinase regulatory subunit type II was performed with the use of two rabbit antisera elicited to a free R-subunit from pig brain and to a RcAMP complex. Quantitative precipitation of the homogeneous antigen revealed six determinants on the R-molecule. Of these at least one is localized in the R-fragment (37 kD), the others--in the N-terminal part of the R-molecule. The antigenic determinants seem to be remoted from the cAMP-binding centers, since the attachment of the affinity purified antibody Fab-fragments to the R-subunit did not influence the cAMP-binding activity of the latter. The antibodies to RcAMP caused dissociation of the holoenzyme. The antibody Fab-fragment binding to the R-subunit prevented its association with the catalytic subunit. The results of immunochemical analysis suggest that the R-subunit adopts different conformations when bound to cAMP or to the catalytic subunit.
Grozdova
I D
ID
Niupenko
E V
EV
Sveshnikova
E V
EV
D000494:Allosteric Regulation; D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D001921:Brain / Q000201:enzymology*; D002384:Catalysis; D000242:Cyclic AMP / Q000378:metabolism*; D000939:Epitopes / Q000032:analysis; D007120:Immunochemistry; D046911:Macromolecular Substances; D011494:Protein Kinases / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D013552:Swine
D000939:Epitopes; D046911:Macromolecular Substances; D000242:Cyclic AMP; D011494:Protein Kinases
Immunokhimicheskie svoĭstva reguliatornoĭ sub''edinitsy cAMP-zavisimoĭ proteinkinazy II tipa.