Figure 2
Figure 2. Effect of band 3 isoforms on Hb-O2 equilibrium. (A) Hb-oxygen dissociation curves were measured for Hb alone (a) or Hb in the presence of wild-type cdb3 (b), kidney cdb3 (c), or GST-(872-911) (d). Hb (20 nmol) was mixed in a cuvette with 10 nmol of cdb3 in a total volume of 200 μl in 10 mM bis-Tris acetate buffer, pH 6.5. After 3 minutes' incubation at 37°C, 2.3 mL of 10 mM bis-Tris acetate buffer, pH 6.5, 20 μl of 20% (w/v) bovine serum albumin, and 8 μl of antifoam solution were added to the solution. Hb-O2 dissociation curves were then generated in a HEMOX analyzer. (B) Graphic comparison of P50 values in the presence and absence of the above band 3 isoforms (error bars represent 1 SD).

Effect of band 3 isoforms on Hb-O2 equilibrium. (A) Hb-oxygen dissociation curves were measured for Hb alone (a) or Hb in the presence of wild-type cdb3 (b), kidney cdb3 (c), or GST-(872-911) (d). Hb (20 nmol) was mixed in a cuvette with 10 nmol of cdb3 in a total volume of 200 μl in 10 mM bis-Tris acetate buffer, pH 6.5. After 3 minutes' incubation at 37°C, 2.3 mL of 10 mM bis-Tris acetate buffer, pH 6.5, 20 μl of 20% (w/v) bovine serum albumin, and 8 μl of antifoam solution were added to the solution. Hb-O2 dissociation curves were then generated in a HEMOX analyzer. (B) Graphic comparison of P50 values in the presence and absence of the above band 3 isoforms (error bars represent 1 SD).

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