A preparation of coagulation factors II, VII, IX, and X was obtained by adsorption onto Al (OH)3 from normal plasma. The subsequent eluate was subjected to gel filtration experiments. It was noticed that the purification obtained on Sephadex G-100 columns was hardly dependent upon the characteristics of the buffer. Factor VII is partly separated from the other factors. Factors II and IX appear to be of equal size, whereas factor X is slightly larger. Molecular weights of about 72,000–74,000 were calculated for factors II, IX, and X, and 57,000–59,000 for factor VII. The coagulation factors are bound to dextran blue, depending upon the ionic strength. Factors II and IX are much more tightly bound than factors VII and X. At an ionic strength of 0.15 and pH 7.0, both, factor II and factor IX interact strongly with dextran blue, whereas the other factors remain free. On the basis of this effect, nearly complete separation can be achieved. The interaction between the factors and dextran blue decreases with increasing pH.

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