Abstract
Modulation of the oxygen equilibria of human fetal and adult hemoglobins by 2,3-diphosphoglyceric acid.
Highlights
Globin (HbF) is lower than thatofnormal human adult X-ray crystallographic studies [7]showed that 1molecule of hemoglobin (HbA) between pH 4 and 8
That of HbA above pH6.9 but, below this pH, the 0 2 it is unclear which of the charged groups interacts affinity of HbF remains lower than thatof HbAeven in to form salt bridges
The pK values of the basic groups of the presence of diphosphoglyceric acid (DPG).These results can be explained by assuming that Val 1y forms a salt bridge with one of the ionized phosphate groups of DPG and His
Summary
From theSecond Departmentof Physiology, Nara MedicalCollege Kashihara, Nara634,Japan. Globin (HbF) is lower than thatofnormal human adult X-ray crystallographic studies [7]showed that 1molecule of hemoglobin (HbA) between pH 4 and 8. Addition of 1 the negatively charged DPG binds in a central cavity between mol of 2,3-diphosphoglyceric acid (DPG)/mol of hemo- two p subunits by forming salt bonds with the positively globin causes the affinity of HbF to be greater than charged residues Val ID, His 2p, Lys 82p, and His 143D. That of HbA above pH6.9 but, below this pH, the 0 2 it is unclear which of the charged groups interacts affinity of HbF remains lower than thatof HbAeven in to form salt bridges. The present study comprises a reexamination of the effect of DPG on the functional properties of fetal hemoglobin at higher thanthat of Val 18
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