[Mechanism of action of cAMP-dependent protein kinase. IV. Interaction of the enzyme catalytic subunit with structural analogs of histone H1].
A study was made of the specificity of the catalytic subunit of cAMP-dependent pig brain protein kinase with respect to structural analogs of the protein substrate, histone H1, namely: a) high-molecular-weight histone fragments obtained as the result of specific cleavage of histone with trypsin and N-bromsuccinimide; b) synthetic peptides-substrates; c) synthetic peptides-inhibitors. Analysis of the kinetic parameters estimated for these compounds allowed to evaluate the individual contribution of various elements of the primary and three-dimensional structure of histone in the processes of binding and phosphorylation. Factors of "near" and "remote" specificity in the protein substrate binding are suggested.
D000818:Animals; D002384:Catalysis; D002417:Cattle; D006657:Histones / Q000378:metabolism*; D007700:Kinetics; D010455:Peptides / Q000378:metabolism; D010766:Phosphorylation; D011487:Protein Conformation; D011494:Protein Kinases / Q000378:metabolism*; D013379:Substrate Specificity; D013552:Swine
D006657:Histones; D010455:Peptides; D011494:Protein Kinases
Mekhanizm deĭstviia cAMP-zavisimoĭ proteinkinazy. IV. Vzaimodeĭstvie kataliticheskoĭ sub''edinitsy fermenta so strukurnymi analogami gistona H1.