Further details are given concerning the movements of proteins on filter paper using 0.1 M. solns. of sucrose and NaK tartrate as developing solvents in the 1st and 2d dimensions, respectively. Mixtures of proteins, such as serum albumin and cytochrome c, may be separated from each other on paper, since the former moves in the 1st dimension, while the latter does not and both proteins move in the 2d dimension. The amt. of cytochrome c moving in the 2d dimension is proportional to the amt. applied to the paper. The chromatographic patterns of purified proteins e.g. crystalline human serum albumin, alpha-, beta-, and gamma-globulins, and fibrinogen differ from each other in a character-istic manner. The differences are more marked when the proteins are mixed with surface active agents with which they form complexes; and these complexes move at different rates on filter paper. Complexes of surface active agents with albumin move with greater ease along the 1st dimension than those formed with globulins; the latter tend to remain at the point of origin. Almost all the protein complexes, however, move in the 2d dimension. The pattern given with a blood plasma is a composite of the patterns of the individual protein fractions, the basal fractions being apparently due to globulin. The patterns of chromatograms of pathological cases (multiple myeloma, liver cirrhosis, cancer of the stomach, lupus erythematosis) differ significantly from the normal, and are often characterized by the presence of heavy basal fractions due probably to increase in the globulin content of the plasma. The chromatograms of dried snake venoms (cobra, Russel viper, Agkistrodon piscivorus) show various distinctive features.