Structural and functional studies of Hb rothschild β 37 (C3) TRP → ARG A new variant of the α<sub>1</sub>β<sub>2</sub> contact

Gâcon, Gérard; Belkhodja, O; Wajcman, Henri; Labie, Dominique; Najman, A

doi:10.1016/0014-5793(77)80593-0

Cited by 53 publications

(26 citation statements)

References 10 publications

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“…This is probably due to the weakened intersubunit interactions in Hb Bassett. Hemoglobin Rothschild (b37 Trp!Arg), which has a substitution at the a1:b2 interface, is also characterized by having low cooperativity, low oxygen affinity, and decreased stability of both the T and R states [30][31][32][33]. Other Hb variants with low cooperativity and low oxygen affinity have been reported by Imai [34].…”

Section: Discussionmentioning

confidence: 99%

Characterization of hemoglobin bassett (α94Asp→Ala), a variant with very low oxygen affinity

et al. 2004

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Hemoglobin (Hb) Bassett, an abnormal Hb variant with a markedly reduced oxygen affinity, was discovered in a Caucasian (Anglo-Saxon) male child who experienced episodes of cyanosis. Cation-exchange and reversed-phase (RP) high-performance liquid chromatography (HPLC) showed that the patient has an abnormal Hb, with a mutation in the a-globin. Tryptic peptide digest of the abnormal a-globin with subsequent HPLC analysis revealed abnormal elution of the a-T11 peptide. Further studies with Edman sequencing and electrospray mass spectrometry of tryptic peptide a-T11, as well as structural analysis by X-ray crystallography revealed an AspfiAla substitution at the a94 (G1) position, a match for Hb Bassett. Detailed functional studies showed that this Hb variant had a markedly reduced oxygen affinity (P 50 at pH 7.0 = 22 mmHg; Hb A P 50 = 10.5 mmHg), reduced Bohr effect (-0.26 compared to -0.54 in Hb A), and low subunit cooperativity (n = 1.4, compared to 2.6 in Hb A). X-ray crystallography results explain the probable effects of the structural modification on the oxygen-binding properties of this Hb variant. Am.

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Section: Discussionmentioning

confidence: 99%

Characterization of hemoglobin bassett (α94Asp→Ala), a variant with very low oxygen affinity

et al. 2004

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“…24 The eluted peaks were subjected to complete mathematical analysis. The standards used to determine the positions of the tetramer, dimer, and monomer in Figure 2 were Hb crosslinked between the N-terminal residues of the a-subunits by a diisothiocyanatobenzene sulfonic acid, 9,10 dimeric Hb Rothschild, 25 and the hydroxymercuribenzoate derivative of the isolated a-subunits, respectively. 15,26 …”

Section: High-resolution Gel Filtrationmentioning

confidence: 99%

Developmental expression of human hemoglobins mediated by maturation of their subunit interfaces

et al. 2010

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Different types of human hemoglobins (Hbs) consisting of various combinations of the embryonic, fetal, and adult Hb subunits are present at certain times during development representing a major paradigm of developmental biology that is still not understood and one which we address here. We show that the subunit interfaces of these Hbs have increasing bonding strengths as demonstrated by their distinct distribution of tetramers, dimers, and monomers during gel filtration at very low-Hb concentration. This maturation is mediated by competition between subunits for more favorable partners with stronger subunit interactions. Thus, the protein products of gene expression can themselves have a role in the developmental process due to their intrinsic properties.

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“…All these haemoglobins show high°2 affinity and diminished haem-haem interaction, probably due to a low L-allosteric constant in the conditions of the isoelectric focusing. Hb Kempsey was studied by Bunn et al (1974), Hb Hotel Dieu by Blouquit et al (1980), Hb Rothschild by Gacon et al (1977) and the mixed-valency hybrids by Rollema et al (1976 Table 4. Values ofpl (ox.)…”

Section: Preparation Ofthe Haemoglobin Solutionsmentioning

confidence: 99%

“…Functional studies in diluted isolated Hb Rothschild solutions have revealed that this mutant haemoglobin has a lower affinity for°2 than has HbAo, small co-operativity in 2 binding and a diminished alkaline Bohr effect (Gacon et al, 1977). At very low concentration of chloride Hb Rothschild keeps its low 02 affinity and low co-operativity, but with a complete inhibition of the alkaline Bohr effect (H. Wajcman & G. Gacon, personal communication).…”

Section: Preparation Ofthe Haemoglobin Solutionsmentioning

confidence: 99%

The measurement of the intrinsic alkaline Bohr effect of various human haemoglobins by isoelectric focusing

Poyart¹,

Guesnon²,

Bohn³

1981

Biochemical Journal

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We have used isoelectric focusing to measure the differences between the pl values of various normal and mutant human haemoglobins when completely deoxygenated and when fully liganded with CO. It was assumed that the Apl(deox. -ox.) values might correspond quantitatively to the intrinsic alkaline Bohr effect, as most of the anionic cofactors of the haemoglobin molecule are 'stripped' off during the electrophoretic process. In haemoglobins known to exhibit a normal Bohr coefficient (AlogP50/ApH) in solutions, the ApI (deox. -ox.) [(1980), J. Mol. Biol. 138, 649-6701 for the mechanism of the alkaline Bohr effect, and also indicate that the transition between the two quaternary configurations is a prerequisite for the full expression of the alkaline Bohr effect.Among the different functional properties of to the peripheral tissues and the homoeostatic mammalian haemoglobins the alkaline Bohr effect is regulation of pH of extracellular fluids. However, of particular interest, as it concerns both 02 delivery despite its extensive study for more than 30 years, its Abbreviations used: Hb, haemoglobin; P50, partial molecular mechanism is still controversial (Kilpressure of 02 at half-saturation of haemoglobin; Bistris, martin et al., 1973;Matthew et al., 1979

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Structural and functional studies of Hb rothschild β 37 (C3) TRP → ARG A new variant of the α₁β₂ contact

Cited by 53 publications

References 10 publications

Characterization of hemoglobin bassett (α94Asp→Ala), a variant with very low oxygen affinity

Characterization of hemoglobin bassett (α94Asp→Ala), a variant with very low oxygen affinity

Developmental expression of human hemoglobins mediated by maturation of their subunit interfaces

The measurement of the intrinsic alkaline Bohr effect of various human haemoglobins by isoelectric focusing

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Structural and functional studies of Hb rothschild β 37 (C3) TRP → ARG A new variant of the α1β2 contact

Cited by 53 publications

References 10 publications

Characterization of hemoglobin bassett (α94Asp→Ala), a variant with very low oxygen affinity

Characterization of hemoglobin bassett (α94Asp→Ala), a variant with very low oxygen affinity

Developmental expression of human hemoglobins mediated by maturation of their subunit interfaces

The measurement of the intrinsic alkaline Bohr effect of various human haemoglobins by isoelectric focusing

Contact Info

Product

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Structural and functional studies of Hb rothschild β 37 (C3) TRP → ARG A new variant of the α₁β₂ contact