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The changes in the partition coefficient of model proteins (lysozyme, myoglobin, conalbumin, bovine serum albumin) in an aqueous two-phase system formed by polyethylene glycol and dextran were examined in order to improve the capacity of counter current distribution for the protein fractionation and concentration. The protein distribution patterns in CCD with 30 tubes varied with the pH of the system, and both theoretical and measured values agreed well. From the mixture of model protein, pure BSA fraction was appeared at the upper-phase of 14th tube having pH 4.5, pure myoglobin at the lower-phase of the 16th tube with pH 6.5 and conalbumin at the lowerphase of 4th tube with pH 12. The result indicated the possible use of CCD method for protein fractionation, if the partition coefficient of proteins was manipulated by pH and other means.
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