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Enzymatic Phosphorylation of Fish Phosvitin

From the ¹ From The Rockefeller University, New York, New York 10021

As reported in the preceding paper, discrete fractions containing increasing amounts of phosphate were isolated from ling roe. The more highly phosphorylated fractions were found to be good acceptors of phosphate from protein phosphokinase and adenosine triphosphate. In contrast to hen phosvitin, enzymatic dephosphorylation lowered the reactivity as phosphate acceptor.

With ling phosvitin and also, apparently, with hen phosvitin, enzymatic phosphorylation by protein phosphokinase and ATP causes a stepwise addition to new phosphate levels. A possible connection to the presence of rather large blocks of serine phosphate in phosvitins is suggested to explain their acceptor specificity.

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