PMID: 6165143Feb 1, 1981Paper

Glycoprotein-sialyltransferase activity of normal human, thrombasthenic and Bernard-Soulier platelets

Vox Sanguinis
B BauvoisJ P Caen

Abstract

Some properties of the sialyltransferase activity of homogenates prepared from normal human platelets were investigated using asialo-fetuin as substrate. The enzyme activity was optimal at pH 6.5 and was stimulated by divalent cations in the order Mg2+ greater than Mn2+ greater than Ca2+. Buffers of high ionic strength strongly reduced the activity. ATP and ADP were not inhibitors at 0.1 mM concentration, but AMP, CTP and CMP reduced the activity by 15-30%. A native endogenous acceptor for the enzyme activity was located in the platelet homogenates. The range of fetuin-sialyltransferase activity found in platelets isolated from 6 normal donors was 79 +/- 39 pmol/h/mg protein (mean +/- SD). The platelets of patients with Glanzmann's thrombasthenia and the Bernard-Soulier syndrome, which are characterized by different membrane glycoprotein deficiencies, were shown to have fetuin-sialyltransferase activities within the normal range indicating that the membrane glycoprotein defects in the platelets of these patients are not associated with the absence of sialyltransferase activity.

References

Oct 1, 1974·British Journal of Haematology·A T Nurden, J P Caen
Mar 1, 1969·British Journal of Haematology·K A Gröttum, N O Solum
Oct 1, 1955·Proceedings of the Society for Experimental Biology and Medicine·F WROBLEWSKI, J S LADUE

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Citations

Oct 1, 1988·Biochemical Medicine and Metabolic Biology·P RodríguezR Apitz-Castro

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