In the serum chromatographies of healthy subjects folic acid activity (FAA) was eluted from the column in the same fractions as α2- macroglobulin, transferrin and albumin, in this order quantitatively. Diphenylhydantoin markedly increased the binding of FAA to serum proteins, especially transferrin. A similar pronounced increase took place in myeloma, hyperthyreosis and hepatitis. In osteomyelitis the binding had decreased clearly in all protein fractions. Whenever the serum FAA had fallen below 3.0 ng/ml, all activity was bound to serum proteins. The chromatographic aberrations in FAA distribution following various pathological conditions, were seen mainly in the transferrin and α2-macroglobulin area. No conclusions can as yet be drawn on the basis of the present study concerning the specificity of these aberrations

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