Abstract
A Ca2+- and calmodulin-dependent protein kinase was purified from baker’s yeast to near homogeneity. At pH 7·5 and 0·1 m-NaCl it has a native molecular mass close to 100 kDa, and is a dimer of apparently identical 56 kDa autophosphorylatable subunits. At 60 μm-CaCl2 and with mixed histones as substrate, half-maximal activation required concentrations of beef calmodulin above 1 μm. At 0·14 μm-beef calmodulin the enzyme showed apparent negative cooperativity towards ATP, with limiting apparent K m values of 4 μm and 60 μm ATP. The enzyme has a broad substrate specificity in vitro, including two yeast proteins that yield, respectively, 50 kDa and 200 kDa phosphopolypeptides.
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