HbS, C, E and F each have a charge that is different from Hemoglobin A
due to their amino acid composition.
This suggests that the sulfate binding site in human hemoglobin also serves as a [Cl.sup.-] binding site, and that the amino-terminal [beta]Vall is essential for oxygen-linked [Cl.sup.-] binding to hemoglobin as
well as the [Cl.sup.-]-dependent Bohr effect.
The expected percentage of hemoglobin A
in each unit withdrawn was calculated in an iterative fashion.
The principle of the test is based on the different susceptibilities of hemoglobin A
(HbA, the major component of adult hemoglobin) and hemoglobin F (HbF, the major component of fetal/ newborn hemoglobin) to alkaline denaturation.
They found that the mean proportion of hemoglobin F to hemoglobin A
(adult) in 59 SIDS victims was 63 percent, compared with a mean of 48 percent in 40 age-matched control infants.