American Society of Hematology

Fig. 4.

$Fig. 4. Comparison of Triton X-100 extractibility of the Rh complex from normal and 4.2(-)HS red blood cells. / Human erythrocyte ghosts (G) were extracted with 1% Triton X-100, and the soluble (S) and insoluble (pellet, P) fractions were analyzed by immunoblotting. (A) As a control of extraction, red Ponceau staining of the nitrocellulose membrane revealed the expected fractionation of proteins between the soluble (*) and pellet (**) pools, with band 3 (***) in both fractions. (B) Immunostaining of Rh complex proteins was performed as described in the legend to Figure 1A. Anti–Duffy MAb was used as a control of membrane solubilization efficiency. Anti-p55 was used as a control of the protein amount loaded for each normal and variant sample.$

Comparison of Triton X-100 extractibility of the Rh complex from normal and 4.2(-)HS red blood cells.

Human erythrocyte ghosts (G) were extracted with 1% Triton X-100, and the soluble (S) and insoluble (pellet, P) fractions were analyzed by immunoblotting. (A) As a control of extraction, red Ponceau staining of the nitrocellulose membrane revealed the expected fractionation of proteins between the soluble (*) and pellet (**) pools, with band 3 (***) in both fractions. (B) Immunostaining of Rh complex proteins was performed as described in the legend to Figure 1A. Anti–Duffy MAb was used as a control of membrane solubilization efficiency. Anti-p55 was used as a control of the protein amount loaded for each normal and variant sample.

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