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Investigation of sickle-cell haemoglobin polymerisation under electrochemical control.

Iqbal Z, Li M, McKendry R, Horton M, Caruana DJ - Chemphyschem (2013)

Bottom Line: The polymerisation was monitored as a change in turbidity during the depletion of oxygen in a small volume custom-built thin-layer electrochemical cell.The cell allowed the investigation of HbS polymerisation as a function of HbS concentration, temperature and solution pH.We confirm that the oxygen was efficiently depleted using finite-element modelling to accurately recreate the electrochemical thin-layer cell.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemistry, University College London, 20 Gordon St., London, WC1 H 0AJ, UK.

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Turbidity–time traces at 700 nm with increasing HbS concentrations between 0 and 200 s, inset showing to 1000 s. Experimental conditions: HbS concentration: a) 100 mg cm−3; b) 75 mg cm−3; c) 50 mg cm−3; d) 40 mg cm−3; e) 30 mg cm−3; f) 20 mg cm−3; g) 100 mg cm−3 of HbA. 1.5 m (pH 7.0) phosphate buffer; 0.5 m NaCl; T=38 °C; E=−0.55 V vs Ag/AgCl.
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fig02: Turbidity–time traces at 700 nm with increasing HbS concentrations between 0 and 200 s, inset showing to 1000 s. Experimental conditions: HbS concentration: a) 100 mg cm−3; b) 75 mg cm−3; c) 50 mg cm−3; d) 40 mg cm−3; e) 30 mg cm−3; f) 20 mg cm−3; g) 100 mg cm−3 of HbA. 1.5 m (pH 7.0) phosphate buffer; 0.5 m NaCl; T=38 °C; E=−0.55 V vs Ag/AgCl.

Mentions: The effect of increasing HbS protein concentration on turbidity, which is an indication of protein aggregation, at a Pt surface was investigated by performing experiments at protein concentrations between 20 mg cm−3 and 100 mg cm−3 at 38 °C. Figure 2 shows the effect of protein concentration on the turbidity change at a wavelength of 700 nm (all other wavelengths showed a similar trend), including 100 mg cm−3 of HbA as a control experiment.


Investigation of sickle-cell haemoglobin polymerisation under electrochemical control.

Iqbal Z, Li M, McKendry R, Horton M, Caruana DJ - Chemphyschem (2013)

Turbidity–time traces at 700 nm with increasing HbS concentrations between 0 and 200 s, inset showing to 1000 s. Experimental conditions: HbS concentration: a) 100 mg cm−3; b) 75 mg cm−3; c) 50 mg cm−3; d) 40 mg cm−3; e) 30 mg cm−3; f) 20 mg cm−3; g) 100 mg cm−3 of HbA. 1.5 m (pH 7.0) phosphate buffer; 0.5 m NaCl; T=38 °C; E=−0.55 V vs Ag/AgCl.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4016751&req=5

fig02: Turbidity–time traces at 700 nm with increasing HbS concentrations between 0 and 200 s, inset showing to 1000 s. Experimental conditions: HbS concentration: a) 100 mg cm−3; b) 75 mg cm−3; c) 50 mg cm−3; d) 40 mg cm−3; e) 30 mg cm−3; f) 20 mg cm−3; g) 100 mg cm−3 of HbA. 1.5 m (pH 7.0) phosphate buffer; 0.5 m NaCl; T=38 °C; E=−0.55 V vs Ag/AgCl.
Mentions: The effect of increasing HbS protein concentration on turbidity, which is an indication of protein aggregation, at a Pt surface was investigated by performing experiments at protein concentrations between 20 mg cm−3 and 100 mg cm−3 at 38 °C. Figure 2 shows the effect of protein concentration on the turbidity change at a wavelength of 700 nm (all other wavelengths showed a similar trend), including 100 mg cm−3 of HbA as a control experiment.

Bottom Line: The polymerisation was monitored as a change in turbidity during the depletion of oxygen in a small volume custom-built thin-layer electrochemical cell.The cell allowed the investigation of HbS polymerisation as a function of HbS concentration, temperature and solution pH.We confirm that the oxygen was efficiently depleted using finite-element modelling to accurately recreate the electrochemical thin-layer cell.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemistry, University College London, 20 Gordon St., London, WC1 H 0AJ, UK.

Show MeSH
Related in: MedlinePlus