Abstract
ATP-depleted human red cells have been incubated in a glucosecontaining medium with ortho [ 32P] phosphate in the presence and in the absence of cyclic AMP and dibutyril cyclic AMP. Then pyruvate kinase has been purified to homogeneity. It was found that pyruvate kinase was intensively phosphorylated in the presence of cyclic 3′–5′ AMP and 5 times less in its absence. The phosphorylated site was readily cleaved by subtilisin.
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