Abstract
Evidence for cell surface protein kinases as possible regulatory factors of cell interaction in Dictyostelium discoideum was examined by incubating intact cells with γ 32P-ATP in the presence and absence of histone. No significant incorporation of 32P was detected in the absence of histone. In its presence strong phosphorylation not only of the histone but also of endogenous proteins was obtained. This was due to the fact that histone made the cell membranes permeable for substrates and proteinkinases. Histone also preserved protein kinase activities which were otherwise lost during homogenization. The total protein kinase activity in histone treated cells was 5 fold higher than in sonicated cells.
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