Gel filtration has been investigated as a method for the fractionation of chick lens proteins using media with a wide range of exclusion limits. The most effective single medium was polyaerylamide with an exclusion limit of 3 × 105 (Bio-Gel P-300). The best separations were obtained by the use of two media in series; polyacrylamide beads with an exclusion limit of 1·5 × 105 (Bio-Gel P-150) followed by agarose beads with an exclusion limit of 1·5 × 106 (Bio-Gel A 1·5 M). A preparative procedure is suggested for the three major classes of chick lens proteins, and the patterns obtained from these classes by immuno-electrophoresis and disc electrophoresis on polyacrylamide are described. The γ-crystallins appeared to be protected from oxidation during preparation by the presence of 10 mm 2-mereaptoethanol. © 1968.