1983
DOI: 10.1007/bf01025235
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Dependence of reactivity and cooperativity in normal human erythrocyte glucose-6-phosphate dehydrogenase on ionic strength, pH, and temperature

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Cited by 4 publications
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“…However, it must be established whether the relative inability of trehalose to partition into the membrane/permeate the RBC limited its abilities to protect against the injury at −4°C, or whether its resulting functionality as an impermeant osmotic agent (relative to PEG400) impeded any protection it could impart. With respect to the latter, an increase in RBC shrinkage could promote activation of non-selective, volume-dependent cation channels, leading to high intracellular Cl-concentrations, which would cause intracellular acidification and a further decrease in the activation energy required for the reduction of major RBC antioxidant systems ( Adediran, 1983 ; Huber et al, 2001 ). On the other hand, partitioning of the Lo phase could minimize low temperature-induced aggregation of Lo domains (and the damage that would result from this), while permeation of PEG400 could limit irreversible denaturation of proteins/macromolecules known to be prominent during prolonged supercooled storage through the formation of hydration shells ( Privalov, 1990 ).…”
Section: Discussionmentioning
confidence: 99%
“…However, it must be established whether the relative inability of trehalose to partition into the membrane/permeate the RBC limited its abilities to protect against the injury at −4°C, or whether its resulting functionality as an impermeant osmotic agent (relative to PEG400) impeded any protection it could impart. With respect to the latter, an increase in RBC shrinkage could promote activation of non-selective, volume-dependent cation channels, leading to high intracellular Cl-concentrations, which would cause intracellular acidification and a further decrease in the activation energy required for the reduction of major RBC antioxidant systems ( Adediran, 1983 ; Huber et al, 2001 ). On the other hand, partitioning of the Lo phase could minimize low temperature-induced aggregation of Lo domains (and the damage that would result from this), while permeation of PEG400 could limit irreversible denaturation of proteins/macromolecules known to be prominent during prolonged supercooled storage through the formation of hydration shells ( Privalov, 1990 ).…”
Section: Discussionmentioning
confidence: 99%