American Society of Hematology

Fig. 2.

$Fig. 2. Detection of PSP in human platelets by immunoblotting. Platelets were lysed in 1% Triton X-100 and the lysate was subjected to SDS-PAGE (2 × 106 cells/lane). (A) Platelet proteins electroblotted to polyvinylidene difluoride membranes were probed with immune (lane 1, 1:500) or preimmune sera (lane 2, 1:500) generated against a peptide sequence of PSP spanning residues 269-277. Relative migration of protein standards (in kilodaltons) is indicated at left. The arrow indicates PSP. (B) Cellular distribution of PSP in platelets. The cellular fractions from human platelets were subjected to SDS-PAGE (2.1 × 106 cells/lane) and immunoblotted with anti-PSP sera. The particulate fractions are shown in lane P. The cytosolic fractions are shown in lane C.$

Detection of PSP in human platelets by immunoblotting. Platelets were lysed in 1% Triton X-100 and the lysate was subjected to SDS-PAGE (2 × 10⁶ cells/lane). (A) Platelet proteins electroblotted to polyvinylidene difluoride membranes were probed with immune (lane 1, 1:500) or preimmune sera (lane 2, 1:500) generated against a peptide sequence of PSP spanning residues 269-277. Relative migration of protein standards (in kilodaltons) is indicated at left. The arrow indicates PSP. (B) Cellular distribution of PSP in platelets. The cellular fractions from human platelets were subjected to SDS-PAGE (2.1 × 10⁶ cells/lane) and immunoblotted with anti-PSP sera. The particulate fractions are shown in lane P. The cytosolic fractions are shown in lane C.

This Feature Is Available To Subscribers Only