The equilibrium between oxygen and sheep haemoglobin at very low percentage saturations

Paul, W.; Roughton, F. J. W.

doi:10.1113/jphysiol.1951.sp004553

Cited by 19 publications

(9 citation statements)

References 4 publications

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“…in process (b) Brooks, 1935) for pH 7-1) in the manner described by Paul & Roughton (1951). The final gas capacity ranged from 0-035 to 0 055 ml.…”

Section: Experimental Methodsmentioning

confidence: 99%

“…Solutions of sheep haemoglobin, at a concentration of 3-4 g Hb/100 ml., have been mainly used, for the reasons previously given by Paul & Roughton (1951).…”

mentioning

confidence: 99%

“…By means of special technique Paul & Roughton (1951) have recently claimed an accuracy of + 0 05 % saturation in the range 0-2 % saturation of haemoglobin with oxygen (i.e. 0-2 O02Hb).…”

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confidence: 99%

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The equilibrium between carbon monoxide and sheep haemoglobin at very high percentage saturations

Roughton¹

1954

The Journal of Physiology

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“…in process (b) Brooks, 1935) for pH 7-1) in the manner described by Paul & Roughton (1951). The final gas capacity ranged from 0-035 to 0 055 ml.…”

Section: Experimental Methodsmentioning

confidence: 99%

“…Solutions of sheep haemoglobin, at a concentration of 3-4 g Hb/100 ml., have been mainly used, for the reasons previously given by Paul & Roughton (1951).…”

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confidence: 99%

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The equilibrium between carbon monoxide and sheep haemoglobin at very high percentage saturations

Roughton¹

1954

The Journal of Physiology

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“…In the case of Valtis & Kennedy (1953, 1954) measurement were made after 30 min equilibration, and with Gullbring & Str6m (1956) after 60 min. A careful and systematic examination of this problem by Paul & Roughton (1951) and Roughton (1954), with haemoglobin in solution, indicated that 30 min shaking is required for equilibration to be complete. With whole blood, particularly when the respiratory function of the erythrocyte is depressed, a corresponding longer period would be necessary.…”

Section: Discussionmentioning

confidence: 99%

The respiratory efficiency and flexibility of erythrocytes stored in acid‐citrate‐dextrose solution

Sirs¹

1969

The Journal of Physiology

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SUMMARY1. Measurements have been made of the flexibility and respiratory efficiency of erythrocytes stored in acid-citrate-dextrose (ACD).2. The rate of packing of stored blood, during centrifugation, indicates that the red blood cells are relatively inflexible.3. Spectrophotometric observations, using the rapid-mixing and stopped-flow technique, indicate that the rate of egress of oxygen from HbO2 in these erythrocytes is significantly reduced. This is not due to a change of the chemical rate of dissociation of HbO2. 4. Neither factor is significantly reversed by resuspending the cells in Ringer-Locke solution or adjusting to pH 7x4. 5. A small improvement is obtained by adding hypertonic NaCl or incubating the blood at 370 C for 1 hr.6. Incubation with adenosine, 25,-mole/ml. blood, at 370 C for at least 1 hr, restored both the respiratory function and flexibility to normal.

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“…It varies with the degree of reaction, has a maximum value at the half way point, and is definitely equal to unity at both extremes. The approach to unity has been observed in the reaction between Hb and oxygen (Paul and Roughton, 1951).…”

Section: Proteins and Hydration Energy-hemoglobin Equilibriamentioning

confidence: 95%

Protein and DNA Reactions Stimulated by Electromagnetic Fields

Blank

2008

LEBM

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The stimulation of protein and DNA by electromagnetic fields (EMF) has been problematic because the fields do not appear to have sufficient energy to directly affect such large molecules. Studies with electric and magnetic fields in the extremely low-frequency range have shown that weak fields can cause charge movement. It has also been known for some time that redistribution of charges in large molecules can trigger conformational changes that are driven by large hydration energies. This review considers examples of direct effects of electric and magnetic fields on charge transfer, and structural changes driven by such changes. Conformational changes that arise from alterations in charge distribution play a key role in membrane transport proteins, including ion channels, and probably account for DNA stimulation to initiate protein synthesis. It appears likely that weak EMF can control and amplify biological processes through their effects on charge distribution.

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The equilibrium between oxygen and sheep haemoglobin at very low percentage saturations

Cited by 19 publications

References 4 publications

The equilibrium between carbon monoxide and sheep haemoglobin at very high percentage saturations

The equilibrium between carbon monoxide and sheep haemoglobin at very high percentage saturations

The respiratory efficiency and flexibility of erythrocytes stored in acid‐citrate‐dextrose solution

Protein and DNA Reactions Stimulated by Electromagnetic Fields

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