Abstract

SummaryDetergent treatment and homogenization enhance adenosine kinase activity but do not affect adenosine deaminase activity in red cell ghosts. Furthermore, adenosine kinase activity is lost during blood storage whereas adenosine deaminase and detergent activation of adenosine kinase are unaffected. Adenosine kinase was not saturated at substrate concentrations as high as 750 μM whereas saturation occurs at 10 μM in intact ghost cells. Finally, adenosine kinase and deaminase activities are not altered by detergent treatment of hemolysates. These findings suggest that membrane disruption exposes previously inaccessible sites for adenosine kinase activity although the possibility of two separate adenosine kinases has not been ruled out.

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