Abstract
Abstract Adenosine kinase has been partially purified from homogenates of rabbit liver and Ehrlich ascites tumor cells. The kinase preparation obtained was free of adenosine deaminase and almost free of adenosine triphosphatase activity. In addition to adenosine, 34 analogues or derivatives of adenosine have been investigated with the enzyme. Of these compounds, 16 were substrates, and the Michaelis constants and maximal velocities of these substrates have been determined. In the presence of myokinase, at least 10 compounds were further phosphorylated to the corresponding triphosphates.
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