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C Poyart

Publications and source records attributed to C Poyart.

At least 181 records · Page 10Linked to original sources
PubMed1979

Interaction of butene with human hemoglobin A.

The binding of various alkanes by proteins was recognized years ago. We have studied the effect of butene (C4H8), a short-chain aliphatic hydrocarbon, on the functional properties of human adult hemoglobin. Under 1 atm pressure (100 kPa) butene decreased the affinity of hemoglobin (Hb) for oxygen (p50) by 45% without altering the cooperativity of ligand binding. This effect was independent of pH (from 7.0 to 8.0) and of ionic strength. The changes in the affinity of hemoglobin for oxygen were dependent upon the partial pressure of butene and evoked a saturating mechanism of the binding site(s). Mathematical simulation of the curve relating p50 to the concentration of dissolved butene allowed us to calculate the apparent association constants for one single binding site KHb = 10.4 mmol-1 and KHbO2 = 1.53 mmol-1 to Hb and HbO2 respectively. The larger binding of butene by Hb was confirmed by a 25% decrease in K1, the first association constant of oxygen to the tetrameric hemoglobin. It is concluded that butene is an allosteric effector of human Hb which acts most likely through hydrophobic interactions. It is postulated that the oxygen-linked binding site may be located at the alpha 1 beta 2 interface.

Alkenes↗
PubMed1979

Comparative effects of CO2 on the affinity for O2 of fetal and adult erythrocytes.

1. Oxygen-linked carbamino formation in fetal erythrocytes was compared to that measured in adult erythrocytes. 2. Whole oxygen binding curves were recorded on washed intact erythrocytes either fresh or D-glycerate-2,3-P depleted with a continuous recording technique. Erythrocytes were resuspended in buffer media of different pH and PCO2 varying from 0-10.7 kPa (80 torr) at physiological ionic strength. Oxygen linked carbamates were estimated as deltalog PO2/delta log PCO2 at constant pH and constant saturation levels from 10-90% oxygen saturation. 3. The overall CO2 effect (deltalog P50/deltalog PCO2) was consistently lower in fetal erythrocytes than in the adult. The deltalog PO2/deltalog PCO2 ratio was markedly dependent on oxygen saturation in both types of erythrocytes and highest at the early part of the oxygen binding curve. This was more so in fetal erythrocytes. 4. Carbamino formation was lower in fetal erythrocytes than in adult erythrocytes at any pH value, indicating a higher apparent pK of the alpha amino groups involved in CO2 binding in fetal erythrocytes. This may be related to the different primary structures of the non alpha chains of HbFII and HbAI. 5. The large effect of low PCO2 on both fetal and adult erythrocytes was related to the higher affinity for CO2 of deoxyhemoglobin compared to oxyhemoglobin and a model for CO2 binding analogous to that described by de Bruin et al. [6] for anion binding is proposed. 6. It is concluded that the lower CO2 binding to fetal erythrocytes is in keeping with the lower allosteric effect of other major effectors of hemoglobin within the cells. This leads to a higher affinity for O2 of fetal erythrocytes well suited for O2 transport in utero.

Adult↗
PubMed1979

The binding of lactate and chloride ions to human adult hemoglobin.

The effects of sodium lactate (Lact) on the oxygen affinity and the Bohr effect of purified human adult hemoglobin solutions have been compared to the effects of sodium chloride (Cl). Changes in the affinity for oxygen have been estimated from the variations of log(O2)50 with pH and at various salt concentration from 0.005 up to 2.0 mol.l-1. (O2)50 was calculated as alpha.P0.5 where alpha is the solubility coefficient of oxygen in the solutions at various salt concentrations. Variations of log(O2)50 with pH at constant salt concentration and variations of log(O2)50 with anion concentration at constant pH have been studied according to the linked-functions theory (Wyman, 1968). Bohr curves and salt binding curves were calculated from standard iterative curve fitting procedures and various parameters relevant to the effects of salts on hemoglobin function were estimated. It is shown that Lact and Cl increase (O2)50 and the alkaline Bohr effect in a comparable way at low salt concentration. At high concentration the effect of Lact predominated over that of Cl. The amount of oxygen linked Lact was larger than that of Cl. Binding constants for both anions to deoxy and oxy Hb were estimated. Lact and Cl have comparable binding constants to deoxy hemoglobin. By contrast Lact binds to oxy hemoglobin to a lesser extent than Cl. This may account for the differences observed in the effects of Lact and Cl on the function of hemoglobin. The reason for the low affinity of oxy hemoglobin for Lact may be related to steric differences between the two anions.

Chemical Phenomena↗
PubMed1979

[Effects of alanine on the metabolism of lactate and glucose in the isolated perfused rat heart (author's transl)].

Perfused non working isolated rat heart preparations have been used to study whether alanine (0,89 gl-1) could represent an energy source for the myocardium. Its influence on glucose and lactate metabolism in the heart was also studied. The use of 14C labelled compounds permitted the estimation of the oxidation rate of these three metabolites. The results show that: 1) Alanine was not utilized by the heart. 2) Alanine did not alter myocardial glucose metabolism or lactate oxidation. 3) Alanine lowered lactate uptake by the myocardium which may indicate that alanine influences lactate transport through the cell membranes. One may speculate that in vivo, alanine will not interfere with glucose or lactate metabolism by the heart as, even in acute physiological conditions (exercice, hypoxie, fasting) lactate is always present in blood at higher concentration than alanine.

Alanine↗
PubMed1978

Chloride binding and the Bohr effect of human fetal erythrocytes and HbFII solutions.

1. We have observed that the alkaline Bohr effect of washed human fetal erythrocytes was larger than in human adult intact red cells, in physiological conditions of pH, PCO2 and temperature. This was also observed independently of the presence of CO2 and of 2,3 diphosphoglycerate (fresh or stored erythrocytes). 2. Experiments performed in purified HbFII and HbA1 solutions and direct titration of protons released upon oxygenation confirmed the larger alkaline Bohr effect of fetal hemoglobin, at physiological ionic strength. 3. At low chloride concentration HbFII solutions had an alkaline Bohr effect identical to that measured in HbA1 solutions. 4. Titration of purified Hb solutions with increasing concentrations of NaCl evidenced a lower O2 linked chloride binding by HbFII and predominantly at acid pH. 5. It is concluded that the larger alkaline Bohr effect of fetal erythrocytes of HbFII solutions is related to a diminished acid Bohr effect, due to the lower affinity of HbFII for chloride anions. 6. The physiological interest of these results for placental O2 transfer (double Bohr effect) and O2 delivery to the foetus is discussed.

Aging↗
PubMed1978

Oxygen transport in children on maintenance haemodialysis.

1. Adaptive mechanisms of oxygen transport by blood have been studied in severely anaemic young patients on maintenance haemodialysis, in conditions of hyperphosphataemia (Pi greater than or equal to 2.2 mmol/l) or normophosphataemia. 2. In hyperphosphataemia whole-blood affinity for oxygen was slightly decreased, as measured by an increase in P50 (the partial pressure of oxygen necessary to half saturate haemoglobin). 2,3-Diphosphoglycerate was increased by 10% (P less than 0.10) whereas Pi, total erythrocyte phosphate and ATP were increased by 100%, 47% and 36% respectively, compared with control values. 3. After correction of hyperphosphataemia a small but significant decrease in P50 and 2,3-diphosphoglycerate, to normal values, was observed whereas the other variables, although significantly lowered, remained above control values. 4. In these severely anaemic and hyperphosphataemic patients P50 and 2,3-diphosphoglycerate are only slightly increased. ATP synthesis appears to be favoured over that of 2,3-diphosphoglycerate. This is possibly due to alterations in the erythrocyte membrane elicited by bi-weekly extracorporeal circulation. Adequate oxygen transport can be achieved only through a drastic increase in blood flow. Correction of hyperphosphataemia adds further to the abnormality. It is concluded that this condition could induce a long-term myocardial fatigue, which might be prevented with occasional small blood transfusions.

Adaptation, Physiological↗
PubMed1978

Hemoglobin Creteil: oxygen transport by erythrocytes. In-vitro and in-vivo studies in a high oxygen-affinity mutant hemoglobin.

Hemoglobin Hb) Creteil alpha2beta(2)89 (F5) Ser leads to Asn is a high oxygen-affinity variant that has a low cooperativity, a decreased Bohr effect, and does not interact with diphosphoglycerate (DPG) (1). This hemoglobin variant was silent by routine electrophoresis. Careful analyses of the oxygen dissociation curves of erythrocytes, determined at varying pH and Pco2 in fresh and DPG-depleted cells, gave extensive information on the abnormal function of the mutant hemoglobin. From the O2 dissociation curves of the erythrocytes of the heterozygous subject it appeared that Hb Creteil is inappropriate for O2 transport to the tissues because it remained completely saturated with O2 at normal physiologic levels of Po2. In-vivo measurements showed that only one half of the total hemoglobin present actually participated in oxygen transport. Polycythemia should therefore be maintained within clinically tolerable limits because it helps to keep arterial Po2 and Pvo2 close to their normal values and thus protects the individual from a permanent increase in blood flow.

Adult↗
PubMed1976

Renal hemodynamics and renal O2 uptake during hypoxia in the anesthetized rabbit.

The effects of hypoxic hypoxia on renal hemodynamics and metabolism have been studied in anaesthetized mechanically ventilated rabbits. Acute hypoxa (FIO2 = 0.10, PaO2 = 35 torr) induces at constant mean arterial pressure a 45% decrease in RBF, GFR, TNa and RVO2 whereas free water clearance increases. These alterations were still apparent 50 min after resuming normal arterial oxygenation. In order to assess the role of the stimulation of catecholamine release in these observations, two other sets of experiments were performed: 1) the animals were ventilated with the same hypoxic gas mixture but after alpha adrenergic blockade (phentolamine: 0.2 mg - kg - min-1 i.v.), 2) hypoxia was induced by ventilating the animals with CO (FICO = 0.002) at constnat PaO2. Increase in renal vascular resistance and reduction of renal O2 uptake were still observed. This indicates that adrenergic stimulation cannot fully explain the renal vasoconstriction encountered in hypoxia. The role of a local vasoactive factor, especially that of the renin angiotensin system is discussed. The apparent O2 cost of Na reabsorption was not greatly modified by any type of hypoxia and the Na: O2 ratio remained close to the value observed in normoxic animals. This indicates that the kidney may adapt to hypoxia by reducing its O2 demand keeping unaltered its tubular function and basal O2 needs.

Animals↗
PubMed1976

Interactions of short chain aliphatic hydrocarbons with human blood and haemoglobin A solutions.

The solubilities of methane, propane, butane and propylene were measured in human whole blood, human plasma and defatted haemoglobin solutions at 37 degrees C. For these four hydrocarbons the solubility coefficient (alpha = ml of gas STPD dissolved in one mal of the solvent under a pressure of one atmosphere) is higher in plasma than in an isoosmolar aqueous solution and higher in whole blood than in plasma. This is due to the presence of proteins and particularly of haemoglobin as shown by the dependence of alpha upon the concentration of haemoglobin in the medium. O2 capacity of human blood is not altered in the presence of these hydrocarbons and its affinity for O2 is slightly decreased.

Air Pollutants↗
PubMed1975

Lactate-glucose interrelations, glucose recycling and the Cori cycle in normal fed rats.

1. Turnover and oxidation rates of glucose and lactate were determined using a priming dose-continuous infusion of 14C-(u)-glucose and 14C-(U)-lactate in anesthetized and mechanically ventilated non-fasted rats. The rates of glucose-lactate interconversions were computed from the two-compartment model of Depocas and De Freitas (1970). The rate of total glucose recycling is known as the difference between the rate of true glucose turnover measured with 3H-(2)-glucose (RGT) and the rate of apparent glucose turnover measured with 14C-glucose (RG). This value was compared with the Cori cycle. 2. In normal conditions 17% of RG come from lactate, 43% are directed to lactate and 49% are oxidized. 3. 71% of the rate of lactate turnover come from glucose, 28% are directed to glucose and 51% are oxidized. 4. The rate of total glucose recycling (RGT-RG) is 3.7 mg - mn(-1) per kg0.75 and represents 60% of RG or 38% of RGT. 5. The Cori cycle is 0.8 - 1.2 mg - mn(-1) per kg0.75 and represents 8 - 20% of the rate of glucose turnover and 20 - 32% of total glucose recycling.

Animals↗