Thromb Haemost 1968; 20(03/04): 366-376
DOI: 10.1055/s-0038-1651279
Originalarbeiten – Original Articles – Travaux Originaux
Schattauer GmbH

A Study of Human Platelet Esterases[*]

E. P Kilburn
1   Department of Medicine, University of Sydney and Clinical Research Unit, Royal Prince Alfred Hospital, Camperdown, N. S. W. Australia
,
B. G Firkin
1   Department of Medicine, University of Sydney and Clinical Research Unit, Royal Prince Alfred Hospital, Camperdown, N. S. W. Australia
› Author Affiliations
Further Information

Publication History

Publication Date:
27 June 2018 (online)

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.

* This work was supported by The Australian Research Grants Committee and presented in part at the XIth Congress of the International Society of Hematology, Sydney, 1966.


 
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