Fatty acylation of human platelet proteins: evidence for myristoylation of a 50 kDa peptide |
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Authors: | M Vidal B Murgue F Bassé A Bienvenüe |
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Affiliation: | URA 530 CNRS, USTL, Montpellier, France. |
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Abstract: | Fatty acid acylation of platelet proteins was studied by measuring incorporation of [3H]palmitate and [3H]myristate after incubation at 37 degrees C for 4 h. About ten major radiolabeled proteins were detected after SDS-polyacrylamide gel electrophoresis and fluorography, for both fatty acids. Cleavage by hydroxylamine treatment indicated an ester bond of either palmitate or myristate to these proteins. Nevertheless, a single 50 kDa peptide was specifically modified by an amide-linked myristate. The functions of acylated proteins in platelets are still unknown, but their relation with DLPC-induced shape changes and vesicle shedding is excluded. |
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