NMR studies of <sup>13</sup>CO‐hemoglobin. α and β chain identification

Antonini, Eraldo; Brunori, Maurizio; Conti, Filippo; Geraci, G.

doi:10.1016/0014-5793(73)80704-5

Cited by 18 publications

(3 citation statements)

References 5 publications

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“…The spectra of Hb trout IV show two well resolved resonances of about the same intensity which can be attributed, as in the case of other hemoglobins, to the two different chains in the tetramer (o-like and P-like chains) [4,5] . Contrary to what observed for all other hemoglobins studied to date, the chemical shift of the r3C0 lines in the Hb trout IV is sensibly pH dependent for both the chains (see figs.1 and 2).…”

Section: Resultsmentioning

confidence: 86%

Observations on CO trout hemoglobins by ¹³C NMR

Giacometti¹,

Giardina²,

Brunori³

et al. 1976

FEBS Letters

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Section: Resultsmentioning

confidence: 86%

Observations on CO trout hemoglobins by ¹³C NMR

Giacometti¹,

Giardina²,

Brunori³

et al. 1976

FEBS Letters

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“…Accordingly we assign the lower field resonance (206.7 ppm) to l3CO bound to the a subunits and the higher field resonance (206.2 ppm) to l3CO bound to the ß subunits of adult and sickle cell carboxyhemoglobins. Antonini et al (1973) have made similar assignments based on separation of HMB derivatized chains, removal of the HMB, and nmr examination of the resulting mercurial-free l3CO a and 13CO ß chains. The mercurial-free 13CO ß chains 2While this manuscript was in the review process, similar results were reported for normal adult carboxyhemoglobin by Vergamini et al (1973).…”

Section: Studies Of Spin-latticementioning

confidence: 95%

Carbon-13 magnetic resonance studies of the binding of carbon monoxide to various hemoglobins

Moon¹,

Richards²

1974

Biochemistry

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“…On the basis of this finding the two types of chain of ) and the P chains (at 206.19 p.p.m.) (Antonini et al, 1973). For the corresponding resonances observed in trout Hb IV (Giacometti et al, 1976) and in aruana Hb (see Fig.…”

Section: Determination Of the C-terminal Residues Of Aruana Haemoglobinmentioning

confidence: 99%

A comparative approach to protein-and ligand-dependence of the Root effect for fish haemoglobins

Giardina

Giacometti

Coletta

et al. 1978

Biochemical Journal

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Ligand-binding equilibria, kinetics and (13)C n.m.r. spectra of bound (13)CO, of the haemoglobins from two fishes that are very distant on the evolutionary scale, i.e. the fourth haemoglobin component from Salmo irideus and the single component from Osteoglossum bicirrhosum, were studied. The C-terminal sequence was also determined for the haemoglobin from Osteoglossum. The results show that (i) the C-terminal residues of both chains are not directly responsible for the characteristic heterotropic effect known as Root effect, since for both fish haemoglobins these residues are identical with those of human haemoglobins. (ii) In all haemoglobins characterized by the Root effect a dependence of the (13)CO n.m.r. resonances on pH is observed. However, the extent of the shift(s) depends on the particular protein, and is probably the result of a combination of both tertiary and quaternary conformational changes. (iii) Both haemoglobins from trout and Osteoglossum manifest a functional heterogeneity between the two types of chains in the tetramer, which increases with proton activity. For CO, the effect is very small for trout haemoglobin IV, and very marked for Osteoglossum haemoglobin; for O(2) strongly heterogeneous binding curves were obtained at approx. pH6.2 with both haemoglobins. (iv) Estimations of the relative values of the affinity constants for the alpha and beta chains in the tetramer were obtained for both haemoglobins from (13)CO n.m.r. spectra at low fractional saturation. On the basis of these findings the molecular mechanism underlying the Root effect is discussed.

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NMR studies of ¹³CO‐hemoglobin. α and β chain identification

Cited by 18 publications

References 5 publications

Observations on CO trout hemoglobins by ¹³C NMR

Observations on CO trout hemoglobins by ¹³C NMR

Carbon-13 magnetic resonance studies of the binding of carbon monoxide to various hemoglobins

A comparative approach to protein-and ligand-dependence of the Root effect for fish haemoglobins

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NMR studies of 13CO‐hemoglobin. α and β chain identification

Cited by 18 publications

References 5 publications

Observations on CO trout hemoglobins by 13C NMR

Observations on CO trout hemoglobins by 13C NMR

Carbon-13 magnetic resonance studies of the binding of carbon monoxide to various hemoglobins

A comparative approach to protein-and ligand-dependence of the Root effect for fish haemoglobins

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Product

Resources

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NMR studies of ¹³CO‐hemoglobin. α and β chain identification

Observations on CO trout hemoglobins by ¹³C NMR

Observations on CO trout hemoglobins by ¹³C NMR