Temperature dependence of the partition coefficient of proteins in aqueous two-phase systems.
We report the partition coefficients of lysozyme, chymotrypsinogen-A, albumin and catalase in sixty four Polyethyleneglycol/Dextran/Water systems at 4, 25 and 40 degrees C. We found that the partition coefficients of the four proteins generally increase with increasing temperature. The influence of temperature on the partition coefficient seems to be highly dependent on the kind of protein which is partitioned and on the total polymer concentration, but does not, in general, depend on the molecular weight of the polymers. The partition coefficients of small and hydrophilic proteins like lysozyme and chymotrypsinogen-A are only slightly affected by changes in temperature, while the partition coefficients of bigger and more hydrophobic proteins like albumin and catalase are strongly affected by changes in temperature. The results suggest the incorporation of attractive forces (possible electrostatic) into a model previously reported by us.
Department of Chemical Engineering, North Carolina State University, Raleigh 27695-7905.
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D000418:Albumins / Q000302:isolation & purification; D002374:Catalase / Q000302:isolation & purification; D002919:Chymotrypsinogen / Q000302:isolation & purification; D009113:Muramidase / Q000302:isolation & purification; D011506:Proteins / Q000302:isolation & purification*; D012995:Solubility; D013696:Temperature
D000418:Albumins; D011506:Proteins; D002919:Chymotrypsinogen; D002374:Catalase; D009113:Muramidase