Temperature independence of the alkaline Bohr effect in pig red cells and pig haemoglobin solutions

Sinet, Martine; Bohn, B.; Guesnon, P; Poyart, Claire

doi:10.1016/0167-4838(82)90209-6

Cited by 8 publications

(5 citation statements)

References 30 publications

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“…From the porcine model, the predicted P 50 was 32.9 Torr. This is consistent with the reported adult porcine P 50 of 32Ϫ34 Torr (4,11,13,15,24,25). In addition, the predicted 99% (P 99 ) and 7.5% saturation with molecular oxygen (P 7.5 ) (the extremes) were, respectively, 150.8 and 14.4 Torr at 37°C and pH 7.4.…”

Section: Resultssupporting

confidence: 90%

“…At the extremes, the limits of saturation were assumed 0 and 100%. Furthermore, because pH and temperature can influence HbO2 binding, correction factors were added to the model (12,21,23,24,26 IL 682 CO-oximeter coefficient determination for porcine blood. Heparinized whole blood was obtained from Yorkshire swine (30-35 kg) and shipped overnight on ice to IL, where it was prepared for the determination of the porcine coefficient set for the IL 682 CO-oximeter.…”

Section: Methodsmentioning

confidence: 99%

“…As with other mammals, porcine hemoglobin has a significant sequence difference from human hemoglobin (5)(6)(7)19). These sequence differences alter the functional properties of hemoglobin and change the electrostatic interactions that modulate the O 2 affinity (24). Subsequently, there is a difference in the HbO 2 saturation characteristics of porcine and human blood as demonstrated by the decreased O 2 affinity of porcine hemoglobin and the resulting increased 50% saturation with molecular oxygen (P 50 ) (2,4,11,15,16,22,25).…”

mentioning

confidence: 99%

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Porcine-specific hemoglobin saturation measurements

Serianni¹,

Barash²,

Bentley

et al. 2003

Journal of Applied Physiology

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The determination of O(2) consumption by using arteriovenous O(2) content differences is dependent on accurate oxyhemoglobin saturation measurements. Because swine are a common experimental species, we describe the validation of CO-oximeter for porcine-specific oxyhemoglobin saturation. After developing a nonlinear mathematical model of the porcine oxyhemoglobin saturation curve, we made 366 porcine oxyhemoglobin saturation determinations with a calibrated blood-gas analyzer and a porcine-specific CO-oximeter. There was a high degree of correlation with minimal variability (r(2) = 0.99, SE of the estimate = 5.2%) between the mathematical model and the porcine-specific CO-oximeter measurements. Bland-Altman comparison showed that the CO-oximeter measurements were biased slightly lower (-0.4 vol%), and the limits of agreement (+/-2 SD) were 0.7 and -1.5 vol%. This is in contrast to a 10-20 vol% error if human-specific methods were used. The results show excellent agreement between the nonlinear model and CO-oximeter for porcine-specific oxyhemoglobin saturation measurements. In contrast, comparison of the porcine-specific oxyhemoglobin saturations with saturations obtained by using human methods highlights the necessity of species-specific measurement methodology.

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Section: Resultssupporting

confidence: 90%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Porcine-specific hemoglobin saturation measurements

Serianni¹,

Barash²,

Bentley

et al. 2003

Journal of Applied Physiology

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“…The distinctive structural features of the chimeric Hbs relative to the parent tetramers is also reflected in their Bohr effect. The Bohr coefficient of swine Hb is nearly 40% lower compared to that of human HbA in 50 mM Bis-Tris acetate buffer at pH 7.0 and 37 "C. Similar observations have been made by Sinet et al (1982), and suggested that the decreased Bohr effect may be due to decreased interactions of the Val-l(a) and . Recently, Katz et al (1994) suggested that A helix of a-subunit shifts away from the protein core by about 0.5 A and a hydrogen bond exists between Val-l(a2) and Asn-13 I(a2).…”

Section: J Rao Et Alsupporting

confidence: 78%

Chimeric hemoglobins — hybrids of human and swine hemoglobin: Assembly and stability of interspecies hybrids

Rao

Acharya

Manjula³

et al. 1996

Protein Science

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“…These hemoglobins have structural and functional differences (see Novy et al 1973;Sinet et al 1982, Rovida et al 1983Shaanan 1983;Uchida et al 1998;Lu et al 2000). The differences in amino acid composition in the a-and b-subunits in these hemoglobins are shown in Table 1.…”

Section: Hemoglobin Samplesmentioning

confidence: 98%

Heme iron state in various oxyhemoglobins probed using Mössbauer spectroscopy with a high velocity resolution

et al. 2011

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A comparative study of oxyhemoglobins from pig, rabbit, normal human and patients with blood system malignant diseases was performed using Mössbauer spectroscopy with a high velocity resolution at 90 K. Mössbauer spectra were fitted with the help of two models: using one quadrupole doublet (model of equivalent iron electronic structure in α- and β-subunits of hemoglobins) and superposition of two quadrupole doublets (model of non-equivalent iron electronic structure in α- and β-subunits of hemoglobins). The results obtained using both models demonstrated small variations of hyperfine parameters that were related to the heme iron state variation in different hemoglobins. These results were compared with structural and functional differences of the hemoglobins investigated.

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Temperature independence of the alkaline Bohr effect in pig red cells and pig haemoglobin solutions

Cited by 8 publications

References 30 publications

Porcine-specific hemoglobin saturation measurements

Porcine-specific hemoglobin saturation measurements

Chimeric hemoglobins — hybrids of human and swine hemoglobin: Assembly and stability of interspecies hybrids

Heme iron state in various oxyhemoglobins probed using Mössbauer spectroscopy with a high velocity resolution

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