American Society of Hematology

Fig. 8.

$Fig. 8. Characterization of solGMR derived from human plasma. / 1 L plasma was applied to an anti-GMRα immunoaffinity column and eluted in 1 mL fractions. Panel A. 40 μL of each fraction was subjected to 10.5% SDS PAGE under reducing conditions and transferred to nitrocellulose. Immunoblotting was performed with biotinylated anti-GMRα antibody SCO4. The number of the fractions is shown above the figure. The position of the molecular weight markers is shown in kilodaltons. Panel B. Fraction 9 was volume reduced to 100 μL and loaded on a Superdex 75 10/30 gel filtration column. Fractions were collected at 1 minute intervals and analyzed in the solGMRα ELISA. The elution position of molecular weight markers is shown in kilodaltons above the graph.$

Characterization of solGMR derived from human plasma.

1 L plasma was applied to an anti-GMRα immunoaffinity column and eluted in 1 mL fractions. Panel A. 40 μL of each fraction was subjected to 10.5% SDS PAGE under reducing conditions and transferred to nitrocellulose. Immunoblotting was performed with biotinylated anti-GMRα antibody SCO4. The number of the fractions is shown above the figure. The position of the molecular weight markers is shown in kilodaltons. Panel B. Fraction 9 was volume reduced to 100 μL and loaded on a Superdex 75 10/30 gel filtration column. Fractions were collected at 1 minute intervals and analyzed in the solGMRα ELISA. The elution position of molecular weight markers is shown in kilodaltons above the graph.

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