The Interaction Between Hemoglobin and Its “Oxygen-Linked” Ligands

Brenna, Oreste V.; Luzzana, M.; Pace, Mario; Perrella, Michele; Rossi, Francesco; Rossi-Bernardi, L.; Roughton, F. J. W.

doi:10.1007/978-1-4684-3222-0_2

Cited by 15 publications

(8 citation statements)

References 19 publications

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“…Table III shows the results obtained when oxygen absorption by hemoglobin was measured in the presence of carbon dioxide with and without benzenepentacarboxylate in solution. It appeared that the combined action of benzenepentacarboxylate and C02 was far from being the sum of the separate effects, in a way similar to that reported for 2,3-diphosphoglycerate and C02 (Bauer, 1969;Pace et al, 1970;Tomita and Riggs, 1971;Brenna et al, 1972). This suggests a competition between C02 and benzenepentacarboxylate similar to that shown between C02 and 2,3-diphosphoglycerate.…”

Section: Interaction Of Benzenepentacarboxylate With Human Fetalmentioning

confidence: 53%

Allosteric effectors of hemoglobin. Interaction of human adult and fetal hemoglobins with poly(carboxylic acids)

Shimizu¹,

Bucci²

1974

Biochemistry

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Aliphatic and aromatic poly(carboxylic acids) interacted with hemoglobin lowering its oxygen affinity. The magnitude of the effect appeared unrelated to the structure of the polyacids and proportional to the number of carboxyl groups present in the compounds. The largest effect was produced by benzenepentacarboxylic acid which at 20°in 0.05 m bis(2-hydroxyethyl)iminotris(hydroxymethyl)methane buffer at pH 7.3 increased log Fy, of human adult hemoglobin from about 0.3 to ca. 1.10 and that of human fetal hemoglobin from ca. 0.5 to ca. 0.95. Its affinity for fetal hemoglobin appeared less than that for adult hemoglobin. It increased the Bohr effect of both hemoglobins, indicating the release, in its presence, of extra protons in addition to those of the alkaline T A he models proposed by Perutz (1970) and Arnone (1972) for the interaction of 2,3-diphosphoglycerate with human hemoglobin show that the 1/3-valines, the 143/3-histidines, and one of the 82/3-lysines form salt bridges with the five negative charges of 2,3-diphosphoglycerate. The 82/3-lysine would interact with the carboxyl group of 2,3-diphosphoglycerate and, according to Arnone (1972), the 2/3-histi dines can also participate in the binding, in this case substituting the 1/3valines. These groups are present in a crevice, between the two ß chains, which only in deoxyhemoglobin is large enough to accommodate 2,3-diphosphoglycerate, thus explaining the preferential binding of 2,3-diphosphoglycerate to this form of hemoglobin (Perutz, 1970).The electrostatic interaction is bound to modify the proton binding behavior of the groups involved, increasing the pK of the positive charges and decreasing that of the negative groups, so that within certain pH ranges hemoglobin is expected to absorb protons upon interaction with 2,3-diphosphoglycerate. This phenomenon contains much information. As it will be discussed in another manuscript, it might help to measure the affinity constant of the effector for hemoglobin, the number of groups which in hemoglobin participate in the interaction, their pK, and their shift to higher pK values in the presence of 2,3-diphosphoglycerate.

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Section: Interaction Of Benzenepentacarboxylate With Human Fetalmentioning

confidence: 53%

Allosteric effectors of hemoglobin. Interaction of human adult and fetal hemoglobins with poly(carboxylic acids)

Shimizu¹,

Bucci²

1974

Biochemistry

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“…which are not identical with the expression found by Brenna et al (1972). The use of eq 27, instead of those of Brenna et al (1972), leads to a considerably different value for the DPG binding constant; Perrella et al (1975) have used eq 26 and 27 to extract DPG binding constants from carbon dioxide binding data.…”

Section: Competitive Binding Of Co2 and Organic Phosphatesmentioning

confidence: 96%

“…Since the binding of CO2 and organic phosphates is competitive, the amount of CO2 bound will decrease in the presence of organic phosphates. The effect of DPG on CO2 binding has been considered by Brenna et al (1972) under the assumption that the binding of DPG and CO2 are mutually exclusive; i.e., if either one or two molecules of CO2 are bound to the ß chains then DPG cannot bind. Since the results obtained for the CO2 binding curve in the presence of phosphates by use of this simplified model are not correct, we present the appropriate expressions here.…”

Section: Competitive Binding Of Co2 and Organic Phosphatesmentioning

confidence: 99%

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Analysis of the interaction of organic phosphates with hemoglobin

Szabó¹,

Karplus²

1976

Biochemistry

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The interaction of organic phosphates with hemoglobin is studied by use of a simple thermodynamic approach. A model-independent analysis is employed to evaluate the accuracy of Adair constants determined in the presence of 2,3-diphosphoglycerate (DPG). The change of oxygen affinity in the presence of phosphates is related to the macroscopic phosphate binding constants of oxy- and deoxyhemoglobin and used to extract such binding constants from oxygen equilibrium measurements. The change of the Bohr effect in the presence of phosphates and the competitive binding of carbon dioxide and DPG are treated quantitatively. The binding of organic phosphates is incorporated into an allosteric model, in which the effect of phosphate on both tertiary and quaternary structure changes is included. By use of this model, the factors which can be responsible for the increased functional heterogeneity of alpha and beta chains in the presence of phosphates are clarified.

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“…The physiological ligands found to be oxygen-linked include pH, carbon dioxide, hydrogen ions, anions of the various salts and certain organic phosphates present in the red cells e. g. 2-3 diphosphoglycerate (2-3 DPG) (1).…”

Section: Discussionmentioning

confidence: 99%

Oxygen Unloading Potential in Bovines in Health and Stress

Singh

Kohli

1980

Zentralblatt für Veterinärmedizin Reihe A

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Summary Oxygen unloading potential (P50) in normal healthy cow calves and buffalo calves was observed to be 26.9 mm. Hg (26.0–29.6 mm. Hg) and 26.2 mm. Hg (24.2–27.5 mm. Hg), respectively. These values were determined from blood pH, pO2, oxygen saturation and base excess. The P50 values were similarly determined in calves following septic shock and uraemia and in buffalo calves under septic shock and after glyceryl guaiacolate administration. The P50 values decreased in uraemic calves and buffalo calves under shock but remained unaffected in the remaining animals. Findings revealed that pCO2 is not specific in shifting the oxygen dissociation curve in bovines, but rather that it interacts with blood pH and other ligands. No correlation could be found between body temperature and the P50 values. Under certain physiopathological conditions, increased base excess in bovines may be disadvantageous as far as oxygen availability to the tissues is concerned. Zusammenfassung Das Sauerstoffabgabevermögen des Hämoglobins bei gesunden und unter Streß stehenden Boviden Bei gesunden Rindern und Büffelkälbern wurde die O2‐Spannung (pO2) für eine 50% O2‐Sättigung des Hämoglobins (P50) bestimmt. Der P50 betrug bei Rinderkälbern 26,9 mm Hg (26,0–29,6 mm Hg) und bei Büffelkälbern 26,2 mm Hg (24,2–27,5 mm Hg). Diese Werte wurden aufgrund des pH, des pO2, der O2‐Sättigung und des Basenüberschusses bestimmt. In analoger Weise wurde der P50 bei Rinderkälbern mit septikämischem Schock und Urämie sowie bei Büffelkälbern mit septikämischem Schock und nach Verabreichung von Glycerolguaiakolat erhoben. Bei Rinderkälbern mit Urämie und Büffelkälbern mit septikämischem Schock sank der P50, bei den übrigen Tieren veränderte sich der P50 nicht. Die Befunde zeigen, daß der pCO2 bei Boviden keinen spezifischen Faktor für die Verschiebung der O2‐Dissoziationskurve darstellt, vielmehr beeinflußt der pCO2 den pH des Blutes sowie andere Faktoren. Zwischen der Körpertemperatur und dem P50 konnte keine Korrelation gefunden werden. Unter gewissen pathologischen Zuständen scheint eine Erhöhung der Pufferbasen (Basenüberschuß) bei Boviden die O2‐Utilisation der Gewebe zu beeinträchtigen. Résumé Capacité de distribution d'oxygène de l'hémoglobine chez des bovins sains et stressés On a déterminé la tension d'O2 (pO2) pour une saturation à 50% de l'hémoglobine chez des veaux de bovins et de buffles sains. Le P50 comprenait 26,9 mm Hg (26,0–29,6 mm Hg) chez les veaux de bovins et 26,2 mm Hg (24,2–27,5 mm Hg) chez les veaux de buffles. Ces valeurs furent déterminées sur la base du pH, du pO2, de la saturation en O2 et de l'excès basique. On a relevé de la même manière la P50 chez des veaux de bovins atteints de choc septicémique et d'urémie et chez des veaux de buffles atteints de choc septicémique et après application de glycéroguaiacolate. Le P50 fut abaisse chez des veaux de bovins atteints d'urémie et des veaux de buffles souffrant de choc septicémique et ne changea pas chez les autres animaux. Les résultats montrent que le pCO2 chez les bovins ne représe...

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The Interaction Between Hemoglobin and Its “Oxygen-Linked” Ligands

Cited by 15 publications

References 19 publications

Allosteric effectors of hemoglobin. Interaction of human adult and fetal hemoglobins with poly(carboxylic acids)

Allosteric effectors of hemoglobin. Interaction of human adult and fetal hemoglobins with poly(carboxylic acids)

Analysis of the interaction of organic phosphates with hemoglobin

Oxygen Unloading Potential in Bovines in Health and Stress

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