Two iron-binding proteins were isolated from rat intestinal mucosa. From determination of their molecular weights, their electrophoretic and iron-binding properties it was established that one was a mucosal ferritin and the other a mucosal transferrin. The mucosal ferritin is compared in its molecular weight, isoelectric point, amino acid composition and tryptic peptide pattern with the ferritins of rat spleen and liver. All three ferritins are distinctly different from one another. In addition the iron content of mucosal ferritin was found to be much lower than that of liver and spleen ferritins. Mucosal transferrin was separated into two components by isoelectric focusing, as was plasma transferrin. The plasma and mucosal transferrins differ in their isoelectric points and in their amino acid compositions. Differences were also found in vitro in the iron-binding of mucosal transferrin as compared with plasma transferrin. The role of these mucosal proteins in the absorption of iron is briefly discussed.