Antibodies to the regulatory subunit of cAMP-dependent protein kinase type II from bovine brain inhibit the holoenzyme formation.

Mouse monoclonal antibodies to the bovine brain regulatory subunit type II (RII) were produced and antibodies of 11 clones were characterized. We determined their subclass, affinity constants, competivity and influence on two RII functions, namely cAMP binding and inhibition of the catalytic subunit (C) activity. 4 clones produced antibodies that increased RII-cAMP binding 1,5-2-fold. Antibodies of other 3 clones prevented R-C association and inhibition of C phosphotransferase activity. Some antibodies affected neither of these RII functions.