1887

Abstract

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

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/content/journal/micro/10.1099/00221287-135-12-3373
1989-12-01
2021-10-24
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