American Society of Hematology

Fig. 3.

$Fig. 3. Distribution of SNAP-23 in resting and activated platelets. / (A) Platelets were resuspended in Ca++-free Tyrode's buffer or Tyrode's (1 mmol/L Ca++) buffer containing 1 U/mL thrombin for 5 minutes. The resting and activated platelets were disrupted by freeze-thaw and fractionated by centrifugation. The supernatant (S1) was collected, and the pellets were washed sequentially with 1 mol/L KCl, 200 mmol/L Na2CO3, and 1% Triton X-100, as in Figure 2(S2, Sc, and Stx). The supernatants and Triton X-100–insoluble pellet (Ptx) were analyzed by Western blotting using ab23 and anti–syntaxin 4 antibody. (B) The Western blotting image was scanned and digitized by using NIH 1.6 program (available at rsb.info.nih.gov/nih.image). The pixel number of each band was normalized as a percentage of total pixel number in all lanes of the treatment group.$

Distribution of SNAP-23 in resting and activated platelets.

(A) Platelets were resuspended in Ca⁺⁺-free Tyrode's buffer or Tyrode's (1 mmol/L Ca⁺⁺) buffer containing 1 U/mL thrombin for 5 minutes. The resting and activated platelets were disrupted by freeze-thaw and fractionated by centrifugation. The supernatant (S1) was collected, and the pellets were washed sequentially with 1 mol/L KCl, 200 mmol/L Na₂CO₃, and 1% Triton X-100, as in Figure 2(S2, Sc, and Stx). The supernatants and Triton X-100–insoluble pellet (Ptx) were analyzed by Western blotting using ab23 and anti–syntaxin 4 antibody. (B) The Western blotting image was scanned and digitized by using NIH 1.6 program (available at rsb.info.nih.gov/nih.image). The pixel number of each band was normalized as a percentage of total pixel number in all lanes of the treatment group.

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