American Society of Hematology

Fig. 7.

$Fig. 7. Targeting of double-mutant procathepsin G to granules in RBL cells. RBL/CatG/Gly201/▵Gly19Glu20 cells were pulse-labeled for 30 minutes followed by chase for 90 minutes and 4 hours. At the times indicated, 100 × 106 cells were homogenized, after which subcellular fractionation was performed, with subsequent collection of eight 0.8 mL subcellular fractions with decreasing density and with fraction no. 9 containing all cytosol. Fractions were solubilized and subjected to immunoprecipitation with polyclonal anti-cathepsin G antiserum. Analyses of immunoprecipitates were as described in the legend to Fig 2. The different processing forms of cathepsin G are indicated with arrows to the right. The fluorograms were exposed for 3 weeks.$

Targeting of double-mutant procathepsin G to granules in RBL cells. RBL/CatG/Gly₂₀₁/▵Gly₁₉Glu₂₀ cells were pulse-labeled for 30 minutes followed by chase for 90 minutes and 4 hours. At the times indicated, 100 × 10⁶ cells were homogenized, after which subcellular fractionation was performed, with subsequent collection of eight 0.8 mL subcellular fractions with decreasing density and with fraction no. 9 containing all cytosol. Fractions were solubilized and subjected to immunoprecipitation with polyclonal anti-cathepsin G antiserum. Analyses of immunoprecipitates were as described in the legend to Fig 2. The different processing forms of cathepsin G are indicated with arrows to the right. The fluorograms were exposed for 3 weeks.

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