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The catalytic (C) subunit of isoenzyme II of cyclic AMP-dependent protein kinase from rat muscle, purified to apparent homogeneity, was investigated for some of its basic properties and factors that influence its activity. The properties were found to resemble those of C subunits of both isoenzymes I and II from various other tissues of different species. This concerns the molecular weight estimate (about 37 k), ultraviolet light absorption spectrum, isoelectric point (pH 9.0 ± 0.2), the apparent K M  values for histone and protamine (for both substrates ≤ 10 μᴍ) and the apparent K M  for cosubstrate ATP (3-4 μᴍ). The enzyme is sensitive to the heat- stable inhibitory protein.

zeitschrift für naturforschung c

Catalytic Subunit of Adenosine Cyclic 3',5' Monophosphate- Dependent Protein Kinase from Rat Muscle: Basic Properties and Factors Influencing the Activity