The a to ß globin chain ratio has been determined in the peripheral red cells of 11 patients with iron deficiency anemia. The mean ratio was found to be 0.74 ± 0.07, which is significantly lower than the ratio of 0.97 ± 0.07 obtained in normals. When the stroma-free hemolysates were purified prior to globin preparation the α to ß ratio did not change. On the other hand, globin extracted from whole iron-deficient cells, including the stroma, had a higher α to ß ratio, 0.88 ± 0.04, but still significantly lower than normal. These results suggest that in iron deficiency there is a decrease in α-chain synthesis relative to ß-chain and that there are membrane-bound globin chains, but no excessive increase in the free α-chain pool. Similar findings have been reported previously in other states of heme deficiency like sideroblastic anemia and lead poisoning.