Journal of Lipid Research, Vol 16, 352-359, Copyright © 1975 by Lipid Research, Inc.
Synthesis of ethanolamine phosphoglycerides by human platelets
FL Call 2d and M Rubert
Platelet homogenates contain an ethanolaminephosphotransferase (EC 2.7.8.1)
that catalyzes the synthesis of ethanolamine phosphoglycerides from
cytidine-5'-diphosphate ethanolamine and 1-radyl-2-acyl-sn- glycerols. The
enzyme is particulate-bound and requires Mn2+ and bile salts for optimal
activity. The apparent Km of the enzyme for cytidine- 5'-diphosphate
ethanolamine is 1.6 X 10(-5) M when the concentration of
1,2-diacyl-sn-glycerols is 8.8 X 10(-4) M. The pH optimum is 8.5 in
Tris-HCl or glycine-NaOH buffer. The activity of the enzyme in platelets
from normal subjects is 0.24-0.34 nmole/min/mg of protein.
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