equilibrium dialysis


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equilibrium dialysis

[‚ē·kwə′lib·rē·əm dī′al·ə·səs]
(analytical chemistry)
A technique used to determine the degree of ion bonding by protein; the protein solution, placed in a bag impermeable to protein but permeable to small ions, is immersed in a solution containing the diffusible ion whose binding is being studied; after equilibration of the ion across the membrane, the concentration of ion in the protein-free solution is determined; the concentration of ion in the protein solution is determined by subtraction; if binding has occurred, the concentration of ion in the protein solution must be greater.
References in periodicals archive ?
Free thyroxine measured by equilibrium dialysis and nine immunoassays in sera with various serum thyroxine-binding capacities.
It is important to note that free T measured by equilibrium dialysis requires a sensitive, specific, precise, and accurate assay for total T.
This was accomplished by progressively diluting serum retentate with serum dialysate (obtained using the equilibrium dialysis method described above).
1) during equilibrium dialysis at 37 [degrees]C by the HEPES acid in dialysate buffer (27).
Ultrafltration devices tested for use in a free thyroxine assay validated by comparison with equilibrium dialysis.
3] concentrations, as determined by equilibrium dialysis, usually remain within reference values, as does the serum TSH concentration.
Traditional measurement procedures separate FTe from the protein-bound Te fraction by equilibrium dialysis (ED) or ultrafiltration (UF).
Established methods that comply fairly well with the above-mentioned requirements are based on equilibrium dialysis (1, 5-7) and ultrafiltration (8-10) followed by quantification of the free hormone by RIA in the dialysate/ ultrafiltrate.
Direct one- and two-step immunoassays are then considered, comparing these in concept and performance with assays ranging from the FTI to the so-called "gold-standard" methods of equilibrium dialysis and ultrafiltration.
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