Oxygen binding and aggregation of hemoglobin from the common European frog, Rana temporaria

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Oxygen binding and aggregation of hemoglobin from the common European frog, Rana temporaria. / Bardgard, A; Fago, A; Malte, H; Weber, R E.

In: Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology, Vol. 117, No. 2, 1997, p. 225-31.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Bardgard, A, Fago, A, Malte, H & Weber, RE 1997, 'Oxygen binding and aggregation of hemoglobin from the common European frog, Rana temporaria', Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology, vol. 117, no. 2, pp. 225-31.

APA

Bardgard, A., Fago, A., Malte, H., & Weber, R. E. (1997). Oxygen binding and aggregation of hemoglobin from the common European frog, Rana temporaria. Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology, 117(2), 225-31.

CBE

Bardgard A, Fago A, Malte H, Weber RE. 1997. Oxygen binding and aggregation of hemoglobin from the common European frog, Rana temporaria. Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology. 117(2):225-31.

MLA

Bardgard, A et al. "Oxygen binding and aggregation of hemoglobin from the common European frog, Rana temporaria". Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology. 1997, 117(2). 225-31.

Vancouver

Bardgard A, Fago A, Malte H, Weber RE. Oxygen binding and aggregation of hemoglobin from the common European frog, Rana temporaria. Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology. 1997;117(2):225-31.

Author

Bardgard, A ; Fago, A ; Malte, H ; Weber, R E. / Oxygen binding and aggregation of hemoglobin from the common European frog, Rana temporaria. In: Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology. 1997 ; Vol. 117, No. 2. pp. 225-31.

Bibtex

@article{a12a1640ce0211dea30a000ea68e967b,
title = "Oxygen binding and aggregation of hemoglobin from the common European frog, Rana temporaria",
abstract = "The hemoglobin from the European frog, Rana temporaria, consists of one major and three minor components. The tetramers aggregate upon deoxygenation notably at pH 7:3. Aggregation due to formation of disulphide bridges, as occurs in related species, was observed only in polyacrylamide gels. The hemolysate showed a pronounced Bohr effect. Oxygen affinity decreased with increasing hemoglobin concentration, indicating that aggregation affects the functional properties of the hemolysate. Oxygen binding equilibria of unfractionated hemolysate are insensitive to chloride and show low sensitivity to ATP. Analysis of oxygen equilibrium curves in terms of the two-state allosteric model (MWC) showed that pH change exerted a greater effect on the association constant of the oxygenated state (KR) than that of the deoxy state (KT). The number of interacting binding sites (q) increased with hemoglobin concentration. Cooperativity of oxygen binding, evaluated as Hill coefficient n, never exceeded the value of 3.0. Earlier studies on hemoglobin and blood from this and related species, report significantly higher n values at high O2 saturation. Molecular adaptive aspects are discussed.",
keywords = "Animals, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Hemoglobins, Hydrogen-Ion Concentration, Isoelectric Focusing, Macromolecular Substances, Mercaptoethanol, Molecular Weight, Oxygen, Pulmonary Gas Exchange, Rana temporaria",
author = "A Bardgard and A Fago and H Malte and Weber, {R E}",
year = "1997",
language = "English",
volume = "117",
pages = "225--31",
journal = "Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology",
issn = "1096-4959",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Oxygen binding and aggregation of hemoglobin from the common European frog, Rana temporaria

AU - Bardgard, A

AU - Fago, A

AU - Malte, H

AU - Weber, R E

PY - 1997

Y1 - 1997

N2 - The hemoglobin from the European frog, Rana temporaria, consists of one major and three minor components. The tetramers aggregate upon deoxygenation notably at pH 7:3. Aggregation due to formation of disulphide bridges, as occurs in related species, was observed only in polyacrylamide gels. The hemolysate showed a pronounced Bohr effect. Oxygen affinity decreased with increasing hemoglobin concentration, indicating that aggregation affects the functional properties of the hemolysate. Oxygen binding equilibria of unfractionated hemolysate are insensitive to chloride and show low sensitivity to ATP. Analysis of oxygen equilibrium curves in terms of the two-state allosteric model (MWC) showed that pH change exerted a greater effect on the association constant of the oxygenated state (KR) than that of the deoxy state (KT). The number of interacting binding sites (q) increased with hemoglobin concentration. Cooperativity of oxygen binding, evaluated as Hill coefficient n, never exceeded the value of 3.0. Earlier studies on hemoglobin and blood from this and related species, report significantly higher n values at high O2 saturation. Molecular adaptive aspects are discussed.

AB - The hemoglobin from the European frog, Rana temporaria, consists of one major and three minor components. The tetramers aggregate upon deoxygenation notably at pH 7:3. Aggregation due to formation of disulphide bridges, as occurs in related species, was observed only in polyacrylamide gels. The hemolysate showed a pronounced Bohr effect. Oxygen affinity decreased with increasing hemoglobin concentration, indicating that aggregation affects the functional properties of the hemolysate. Oxygen binding equilibria of unfractionated hemolysate are insensitive to chloride and show low sensitivity to ATP. Analysis of oxygen equilibrium curves in terms of the two-state allosteric model (MWC) showed that pH change exerted a greater effect on the association constant of the oxygenated state (KR) than that of the deoxy state (KT). The number of interacting binding sites (q) increased with hemoglobin concentration. Cooperativity of oxygen binding, evaluated as Hill coefficient n, never exceeded the value of 3.0. Earlier studies on hemoglobin and blood from this and related species, report significantly higher n values at high O2 saturation. Molecular adaptive aspects are discussed.

KW - Animals

KW - Chromatography, Gel

KW - Electrophoresis, Polyacrylamide Gel

KW - Hemoglobins

KW - Hydrogen-Ion Concentration

KW - Isoelectric Focusing

KW - Macromolecular Substances

KW - Mercaptoethanol

KW - Molecular Weight

KW - Oxygen

KW - Pulmonary Gas Exchange

KW - Rana temporaria

M3 - Journal article

C2 - 9226882

VL - 117

SP - 225

EP - 231

JO - Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology

JF - Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology

SN - 1096-4959

IS - 2

ER -