Fig. 5.
Fig. 5. CD36-associated proteins on thrombasthenic platelets. / Platelet membrane proteins from a patient with Glanzmann thrombasthenia were labeled with biotin and lysed in Brij 99 (lanes 1, 2, and 3) or CHAPS (lanes 4, 5, and 6). The platelet lysates were immunoprecipitated with anti-CD36 antibody FA6-152 (lanes 1 and 4), anti-CD9 antibody (lanes 2 and 5) or nonimmune mouse IgG (lanes 3 and 6). The results show that CD36 was coprecipitated with CD9 and α6β1 in the absence of αIIbβ3. Lane 7 is the complete platelet lysate, showing that multiple platelet membrane proteins are biotinylated and the bands that are immunoprecipitated with anti-CD36 antibodies are not selectively labeled.

CD36-associated proteins on thrombasthenic platelets.

Platelet membrane proteins from a patient with Glanzmann thrombasthenia were labeled with biotin and lysed in Brij 99 (lanes 1, 2, and 3) or CHAPS (lanes 4, 5, and 6). The platelet lysates were immunoprecipitated with anti-CD36 antibody FA6-152 (lanes 1 and 4), anti-CD9 antibody (lanes 2 and 5) or nonimmune mouse IgG (lanes 3 and 6). The results show that CD36 was coprecipitated with CD9 and α6β1 in the absence of αIIbβ3. Lane 7 is the complete platelet lysate, showing that multiple platelet membrane proteins are biotinylated and the bands that are immunoprecipitated with anti-CD36 antibodies are not selectively labeled.

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