Twenty proteins with molecular masses between 10(4) and 10(6) were par
titioned in aqueous dextran-poly(ethylene glycol) two-phase systems wi
th either 0.1 M KC] or 0.1 M KCl plus 3 M NaCl. The partition coeffici
ent of all proteins were higher in the system with 0.1 M KCl plus 3 M
NaCl than in the system with 0.1 M KCl alone. The ratios between the p
artition coefficients in the two systems were strongly correlated with
the molecular masses of the proteins. This fact may be used for analy
tical as well as preparative purposes.