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The ability of porous bodies to distinguish between molecules of different sizes has been repeatedly observed. If these porous bodies are devoid of charged groups, solutes placed on top of a column filled with such a material will be partitioned chiefly by molecular sieve effect (1). Molecules with a size above a limiting value will leave the column immediately after the displacement volume. Smaller particles will enter the gel grains and will be retarded and eventually separated into groups of different molecular weight. Such columns, on the other hand, may perform an exhaustive dialysis. The use of dextran gels for these purposes was introduced by Porath and Flodin (2); as suggested by Tiselius the method was named gel filtration. Nonmetabolized corticoids may be found in human plasma in three different forms: a very small fraction of unbound steroids, a fraction weakly bound to albumin, and a fraction strongly but reversibly bound (3) to a specific protein called transcortin (4). Under basal conditions the latter fraction represents 95 to 98 per cent of total plasma cortisol.1

PROTEIN BINDING OF CORTICOIDS STUDIED BY GEL FILTRATION*