Summary
1. Platelet esterase activity has been estimated using a manometric technique. The most suitable substrate used was tributyrin. Tributyrinase activity corresponded with DFP32 uptake by the platelet and probably reflected overall esterase activity. Evidence has been presented that this enzyme is an integral part of the platelet.
2. Platelet esterase activity rapidly diminished on storage at 4° C and was peculiarly susceptible to cell lysis. This activity may be an index of platelet viability.
3. No direct correlation could be found between platelet esterase activity and platelet aggregation.