The regulatory subunit type II (RII) of cAMP‐dependent protein kinase purified from human brain was represented by two proteins with apparent molecular masses of 51‐52 kD and 54 kD. Dephosphorylation of human RII containing 3 mol phosphate/mol protein did not change the electrophoretic pattern. One‐dimensional peptide mapping of 51‐52 kD and 54 kD proteins after digestion with St. aureus V8 protease evidenced to their being distinct proteins. The data obtained permit to assume that human RII of neural type is represented by two isoforms.

Regulatory subunits type II (RII) purified from human, pig and bovine brains were compared using 11 monoclonal antibodies (MoAb) against bovine brain RII. Bovine RII has at least 5 antigenic sites located in the N‐terminal 1‐110 residues. Immunochemical difference detected between human and animal RII was more pronounced than between pig and bovine RII. Certain MoAb influenced R‐cAMP binding and holoenzyme formation. RII of the three species responded to MoAb attachment in a similar fashion. The results suggest that anchoring of neural protein kinase via the N‐terminal part of RII may influence the enzyme activity.

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БеЗоПасностЬ стерляди, выращенной в условияХ уЗв наумова валентина васильевна, кандидат сельскохозяйственных наук, заведующая кафедрой частной зоотехнии, технологии животноводства и аквакультуры кирьянов дмитрий анатольевич, кандидат сельскохозяйственных наук, доцент кафедры частной зоотехнии, технологии животноводства и аквакультуры свешникова елена васильевна, кандидат биологических наук, доцент кафедры частной зоотехнии, технологии животноводства и аквакультуры

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