Fig. 5. Tyrosine phosphorylation of Syk and PLCγ2 in platelets adherent to decorin. / Samples of total platelets (TOT) and platelets nonadherent (NA) or adherent (A) to decorin were lysed with immunoprecipitation buffer. Aliquots of each sample containing the same amount of proteins (100 μg) were immunoprecipitated with 1 μg of anti-Syk (A) or anti-PLCγ2 (B). Immunoprecipitated proteins were separated by SDS-PAGE on a 7.5% acrylamide gradient gel and transferred to nitrocellulose. Filters were then probed with antiphosphotyrosine antibody (P-Tyr). Upon inhibition of the peroxidase-conjugated secondary antibody with NaN3, the nitrocellulose filters were reprobed with the same antibody used for immunoprecipitation (Syk or PLCγ2). The positions of standard molecular weight markers are reported on the left.
Fig. 5.

Tyrosine phosphorylation of Syk and PLCγ2 in platelets adherent to decorin.

Samples of total platelets (TOT) and platelets nonadherent (NA) or adherent (A) to decorin were lysed with immunoprecipitation buffer. Aliquots of each sample containing the same amount of proteins (100 μg) were immunoprecipitated with 1 μg of anti-Syk (A) or anti-PLCγ2 (B). Immunoprecipitated proteins were separated by SDS-PAGE on a 7.5% acrylamide gradient gel and transferred to nitrocellulose. Filters were then probed with antiphosphotyrosine antibody (P-Tyr). Upon inhibition of the peroxidase-conjugated secondary antibody with NaN3, the nitrocellulose filters were reprobed with the same antibody used for immunoprecipitation (Syk or PLCγ2). The positions of standard molecular weight markers are reported on the left.

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