Interaction between blood components and a spin-labeled analogue of PAF-acether

The interactions between a spin-labeled analogue of PAF-acether (designated as (0,2)PAF) and different human blood components (platelets, erythrocytes, and serum) have been studied. The rate of spin probe reduction by cytosol provided information about the internalization processes when the hydrolysis rate was also available. Although erythrocyte reactivity is lower than that of platelets, erythrocytes, because of their greater numbers, removed (0,2)PAF from whole blood faster than platelets. Lastly, erythrocytes may be more efficient traps for (0,2)PAF than serum acetylhydrolase. Criteria for extending these results to genuine PAF-acether are also discussed.