The binding of lactate and chloride ions to human adult hemoglobin

Guesnon, P; Poyart, Claire; Bursaux, E; Bohn, B.

doi:10.1016/0034-5687(79)90031-8

Cited by 19 publications

(6 citation statements)

References 21 publications

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“…As far as the lactate effect is concerned, it is well known that this ion, like other anions, decreases the oxygen affinity of human haemoglobin A (Guesnon et al, 1979;Amiconi et al, 1981). This effect is particularly evident in the case of whale haemoglobin (see Tables 1 and 2), even if the experiments have been performed in the presence of -200 mM-Clwhich would tend to mask the effect of lactate on haemoglobin oxygen affinity.…”

Section: Vol 271mentioning

confidence: 99%

Temperature modulation of oxygen transport in a diving mammal (Balaenoptera acutorostrata)

Brix

Condò²,

Bardgard

et al. 1990

Biochemical Journal

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The functional properties of haemoglobin from the Lesser Rorqual whale (Balaenoptera acutorostrata) have been characterized as a function of the heterotropic effector concentrations and temperature. The results obtained suggest the existence of sophisticated modulation mechanisms based on the interplay of organic phosphates, carbon dioxide, lactate and temperature. These, together with the very small apparent heat of oxygenation (delta H) of oxygen binding, have been physiologically interpreted on the basis of the specific metabolic needs of this diving mammal.

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Section: Vol 271mentioning

confidence: 99%

Temperature modulation of oxygen transport in a diving mammal (Balaenoptera acutorostrata)

Brix

Condò²,

Bardgard

et al. 1990

Biochemical Journal

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“…The overall apparent association constant of oxygen-linked halothane (Ka) is 3.2 mmol" 1 . This is about half that estimated for butene binding (Poyart et al, 1979) and much less than that of chloride ions (13 mmol"') (Guesnon et al, 1979) or 2, 3-DPG binding (280 mmoP 1 ) (Benesch et al, 1971).…”

Section: Resultsmentioning

confidence: 63%

“…According to the linked-function relationship (Wyman, 1964) this is obtained from the ratio A log P50/A log [halothane] mmol litre"' provided that the oxygen binding curves remain symmetrical in the presence of the factor concerned, and is halothane 0.05 mol per mol haem oxygenated. This quantity is small compared with other factors such as chloride, 0.5 mol at pH 7.0 (Guesnon et al, 1979). From the value of the upper asymptote estimated from the curve shown in figure 1, a Hill plot can be drawn relating the logarithm of the fractional effect to the logarithm of the concentration of halothane (fig.…”

Section: Resultsmentioning

confidence: 99%

Oxygen-Linked Binding of Halothane to Human Adult Haemoglobin

Guesnon

Bohn²,

Bursaux³

et al. 1980

British Journal of Anaesthesia

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The affinity for oxygen of normal human haemoglobin (Hb) solutions was measured in the presence of increasing concentrations of halothane. We observed a maximum increase in P50 of 25% with halothane 40 kPa compared with control (oxygen-argon gas mixtures) indicating the oxygen-linked character of the binding of halothane to the Hb molecule. The effect of halothane on P50 was independent of pH between 7.0 and 8.0 and of chloride concentration between 10 and 100 mmol litre-1. This suggests that halothane-Hb interactions may occur through hydrophobic linkage as occurs with short chain aliphatic hydrocarbons. The oxygen-linked binding of halothane appears of minor importance in altering oxygen binding to Hb in vivo compared with other factors such as chloride ion or 2, 3-DPG.

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“…These water conformations in the whole blood aqueous system may be the result of water-lactate molecular interactions and the formation of ionic lactate complex clusters, as whole blood is a polar solvent that can sustain ionic complexes [33]. It is also possible that bonded lactate structures in aqueous solution were the result of lactate ions bound to plasma proteins [36] or to deoxy-and oxyhaemoglobin [37]. Because of these bound complexes, the effects of concentration change of different free analytes would not be seen in such an aqueous system [38].…”

Section: Spectral Regions With O-h Absorption Interferencementioning

confidence: 99%

Comparison of Dual Beam Dispersive and FTNIR Spectroscopy for Lactate Detection

Baishya

Mamouei

Budidha

et al. 2021

Sensors

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Near Infrared (800–2500 nm) spectroscopy has been extensively used in biomedical applications, as it offers rapid, in vivo, bed-side monitoring of important haemodynamic parameters, which is especially important in critical care settings. However, the choice of NIR spectrometer needs to be investigated for biomedical applications, as both the dual beam dispersive spectrophotomer and the FTNIR spectrometer have their own advantages and disadvantages. In this study, predictive analysis of lactate concentrations in whole blood were undertaken using multivariate techniques on spectra obtained from the two spectrometer types simultaneously and results were compared. Results showed significant improvement in predicting analyte concentration when analysis was performed on full range spectral data. This is in comparison to analysis of limited spectral regions or lactate signature peaks, which yielded poorer prediction models. Furthermore, for the same region, FTNIR showed 10% better predictive capability than the dual beam dispersive NIR spectrometer.

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The binding of lactate and chloride ions to human adult hemoglobin

Cited by 19 publications

References 21 publications

Temperature modulation of oxygen transport in a diving mammal (Balaenoptera acutorostrata)

Temperature modulation of oxygen transport in a diving mammal (Balaenoptera acutorostrata)

Oxygen-Linked Binding of Halothane to Human Adult Haemoglobin

Comparison of Dual Beam Dispersive and FTNIR Spectroscopy for Lactate Detection

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