Fig. 2: Biochemical characterization of purified HbG.
a Oxygen binding affinity comparison between HbA, HbS, and HbG. Traces shown represent a single curve of data collected in quadruplicates. Numbers shown represent the average and standard deviations of Hill coefficients and p50 values calculated from each individual trace. Name in parenthesis indicates source utilized for isolation (Townes-mice blood, h blood-human blood). In vitro polymerization kinetics of purified (b) HbG at various concentrations, (c) HbA:HbS and (d) HbG:HbS mixtures at various HbS percentages at a total hemoglobin concentration of 2 mg/mL. e The relationship between the log of reciprocal delay time and HbS concentration of binary mixtures of either HbA (blue circles) or HbG (red squares) with HbS is shown. Extra sum-of-squares F test was performed to compared both data sets. HbS percentages used for each mixture are shown above their respective data points. Source data are provided as a Source Data file.
