Maximal elevation of 2,3-diphosphoglycerate concentrations in human erythrocytes: Influence on glycolytic metabolism and intracellular pH

Deüticke, B.; Duhm, Jochen; Dierkesmann, R

doi:10.1007/bf00586792

Cited by 81 publications

(23 citation statements)

References 42 publications

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“…DPG exhibited a steady increase throughout the present incubation interval. As already pointed out by DEUTICKE et al (1971), a negative linear correlation was present between the red cell contents of organic phosphates and water. The water loss and the consequent increase in MCHC might result in a decrease of red cell deformability due to an increase in the internal viscosity (WALTER and SITU, 1985).…”

Section: Methodssupporting

confidence: 62%

Incubation procedure effective for decreasing oxygen affinity of red cells in the dog.

et al. 1986

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Because oxygen affinity of canine red cells had been hardly reduced by the conventional procedure of incubation with inosinepyruvate-phosphate or dihydroxyacetone-pyruvate-phosphate, incubation with acidified phosphoenolpyruvate (PEP) medium was tested for its effect on oxygen affinity. As this procedure had been shown to induce a significant increase of 2,3-diphosphoglycerate (DPG) in human red cells, it was also proved to be effective for lowering oxygen affinity of canine red cells. Incubation with 15 mM PEP in ACD medium (pH 6.0) at 37°C for 30 min was the standard procedure established after critical scrutiny. The incubated blood exhibited an average increase in half-saturation pressure (P50) amounting to 7 Torr (pH 7.40, P~02 40 Torr, 37°C), with no appreciable hemolysis and little change in mean corpuscular hemoglobin concentration. Results with Dowex 1-X8 anion exchange chromatography of acid soluble phosphates from the incubated red cells suggested that PEP penetrated rapidly through, the canine red cell membrane and was metabolized to DPG via the retrograde process of the Embden-Meyerhof glycolytic pathway.

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Section: Methodssupporting

confidence: 62%

Incubation procedure effective for decreasing oxygen affinity of red cells in the dog.

et al. 1986

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“…Only a moderate level of Pi is reached in the cells (~4 mM) [39], and this level seems not to affect the binding of 2,3-DPG to the hemoglobin. In fact, no shifts were observed in the 2,3-DPG 31P NMR lines when Pi was added to model solutions [ 191, and the Pi line itself did not shift in intact erythrocytes when the state of the hemoglobin changed from oxy to deoxy.…”

Section: Discussionmentioning

confidence: 92%

“…In fact, no shifts were observed in the 2,3-DPG 31P NMR lines when Pi was added to model solutions [ 191, and the Pi line itself did not shift in intact erythrocytes when the state of the hemoglobin changed from oxy to deoxy. The small increase of the adenosine triphosphate (ATP) level originated by the incubation (-0.2 mM) [39], together with the small percentages of binding of oxyhemoglobin to either ATP or ATP-Mg*+ complex [41], exclude any significant contribution of this compound to the observed shifts. Even assuming that other minor metabolites, such as, adenosine diphosphate (ADP), inosine monophosphate (IMP), 2-phosphoglycerate (2-PG), nicotinamide dinucleotide (NADH), bind to oxyhemoglobin with binding constants of the same order of magnitude as the 2,3-DPG-oxy constant, only a small contribution to the shifts is expected, because of their low concentration (<l mM).…”

Section: Discussionmentioning

confidence: 99%

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¹H NMR study of the binding of 2,3‐diphosphoglycerate to human oxyhemoglobin a in intact red cells

Nieto

1981

FEBS Letters

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“…The intracellular 2,3-DPG content was increased by the method of Deuticke, Duhm & Dierkesmann (1971), i.e. the red cells were washed with 0-9 % NaCl and adjusted to haematocrit (Ht) -45% with saline.…”

Section: Preparation Of 23-dpg-increased Red Cellsmentioning

confidence: 99%

A method for studying oxygen diffusion barrier in erythrocytes: effects of haemoglobin content and membrane cholesterol.

Kon¹,

Maeda²,

Sekiya³

et al. 1980

The Journal of Physiology

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SUMMARY1. In order to study the kinetics of the oxygen egress from human red cells in the 50 sec-20 min time range, an apparatus for measuring the oxygen dissociation process was constructed, combining a spectrophotometer with an oxygen electrode of quick response. 3. The r value was always 1x0 for the haemolysate, but it was less than 1-0 for the normal red cells. Further, the oxygen dissociation curve of red cells obtained at higher Vmax was distorted, due to the non-equilibration between intra-and extracellular oxygen concentrations.4. The r value was (i) independent of the amounts of the allosteric effectors (2,3-diphosphoglycerate and H+) but (ii) dependent on the haemoglobin contents and (iii) dependent on the amounts of the membrane cholesterol. Therefore, the r value reflected only the process of the oxygen diffusion but not the 'chemical reaction' rate. The 'barrier' of the oxygen diffusion decreased at lower haemoglobin contents, but increased at higher cholesterol contents in the membrane.

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Maximal elevation of 2,3-diphosphoglycerate concentrations in human erythrocytes: Influence on glycolytic metabolism and intracellular pH

Cited by 81 publications

References 42 publications

Incubation procedure effective for decreasing oxygen affinity of red cells in the dog.

Incubation procedure effective for decreasing oxygen affinity of red cells in the dog.

¹H NMR study of the binding of 2,3‐diphosphoglycerate to human oxyhemoglobin a in intact red cells

A method for studying oxygen diffusion barrier in erythrocytes: effects of haemoglobin content and membrane cholesterol.

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Maximal elevation of 2,3-diphosphoglycerate concentrations in human erythrocytes: Influence on glycolytic metabolism and intracellular pH

Cited by 81 publications

References 42 publications

Incubation procedure effective for decreasing oxygen affinity of red cells in the dog.

Incubation procedure effective for decreasing oxygen affinity of red cells in the dog.

1H NMR study of the binding of 2,3‐diphosphoglycerate to human oxyhemoglobin a in intact red cells

A method for studying oxygen diffusion barrier in erythrocytes: effects of haemoglobin content and membrane cholesterol.

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¹H NMR study of the binding of 2,3‐diphosphoglycerate to human oxyhemoglobin a in intact red cells