Figure 2.
Figure 2. Two-dimensional electrophoresis of the releasate fraction from thrombin-activated platelets. A total of 400μg of the releasate fraction from thrombin-activated platelets was separated by 2-DE and stained with Coomassie blue dye. Spots were excised and digested with trypsin and the resulting peptides were analyzed by MALDI-TOF MS. A representative gel is shown and the proteins identified are listed (see Table 1). Molecular weight markers and pI values are indicated.

Two-dimensional electrophoresis of the releasate fraction from thrombin-activated platelets. A total of 400μg of the releasate fraction from thrombin-activated platelets was separated by 2-DE and stained with Coomassie blue dye. Spots were excised and digested with trypsin and the resulting peptides were analyzed by MALDI-TOF MS. A representative gel is shown and the proteins identified are listed (see Table 1). Molecular weight markers and pI values are indicated.

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