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Structural and functional studies of hemoglobin poissy



Structural and functional studies of hemoglobin poissy



European Journal of Biochemistry 153(3): 655-662



Homoglobin Poissy .alpha.2.beta.256 (D7) Gly .fwdarw. Arg and 86 (F2) Ala .fwdarw. Pro, is a new variant of the .beta. chain with two substitutions with the second exon of the corresponding gene. The electrophoretic mobilities are identical to those of Hb Hamadan .alpha.2.beta.256 (D7) Gly .fwdarw. ARg as is the fingerprint of the tryptic hydrolysate of the two abnormal .beta. chains. The second substitution .beta.86 Ala .fwdarw. Pro was detected by high-pressure liquid chormatography. Hb Poissy has a threefold increase in oxygen affinity with low Hill coefficient and diminished Bohr effect, which are restored to normal upon addition of 2,3-bisphosphoglycerate. Since the functional properties of Hb Hamadan (.beta.56 Gly .fwdarw. Arg) have been described as normal, the abnormal function of Hb Poissy may be attributed to the .beta.86 (F2) Ala .fwdarw. Pro substitution. Hb Pissy exhibits a mild instability and a greater reactivity of the thiol groups of the .beta.93 (F9) Cys residues in the deoxy form than does Hb A. The oxidation rate of Hb Poissy is biphasic indicating a large inequivalence between the .alpha. and .beta. hemes. Thereafter NMR studies demonstrated that the .beta.86 Ala .fwdarw. Pro substitution produces a displacement of the F helix closer to the heme plane and a large increase in the dynamic fluctuations of the tertiary structure on the proximal side of the .beta. hemes. These results lead to the conclusion that the .beta.86 Ala .fwdarw. Pro substitution produces a destablization of the F helix extending downwards to the FG corner and altering both the .beta. hemes and the .alpha.1.beta.2 contacts.

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Accession: 006489652

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