Journal
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
Volume 42, Issue 5, Pages 413-418Publisher
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s10863-010-9310-y
Keywords
Albumin; Erythrocytes; Osmotic stability; Sodium dodecyl sulfate; Surfactants; Temperature
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Funding
- Fundacao de Amparo a Pesquisa do Estado de Minas Gerais (FAPEMIG)
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The stability of human erythrocytes to sodium dodecyl sulfate (SDS) was assessed spectrophotometrically in the presence of different concentrations of bovine serum albumin (BSA) and at different temperatures (27-45 A degrees C). The absorbance at 540 nm (A (540) ) was correlated with the SDS concentration by sigmoidal regression based on the Boltzmann equation. Erythrocyte stability was characterized on the basis of the SDS concentration that induces hemolysis in 50% of the cells (D (50) ). Progressive increases in the albumin concentration led to increases in the D (50) value. The protective effect of BSA against SDS-induced hemolysis was attributed to the binding of the surfactant to the hydrophobic binding sites of this protein. The D (50) values decreased sigmoidally with an increase in the temperature. This trend, which could not be explained by changes in the spectral properties of hemoglobin, maybe due to heterogeneity in the erythrocyte population.
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