Rat thyroid hemilobes were incubated in presence of exogeneous, heterologous and homologous thyroglobulins. The median density of the thyroglobulin molecules originally added to the medium was compared with that of the molecules remaining at the end of a three‐hour incubation period (37°C). A certain degree of specificity in the reabsorption process of thyroglobulin was found: the uptake of homologous molecules (rat) was higher than heterologous (hog) molecules. The median density of the iodoproteins remaining after the incubation did not change for the heterologous whereas it shifted towards lower density for the homologous thyroglobulins (equilibrium labelled, 35 iodine atoms/molecule). In addition, rat follicular cells display selectivity in the endocytosis of homologous thyroglobulin. Among the rat molecules, the normally iodinated are taken up more actively than the lowly iodinated or newly synthesized ones. Dissimilarity in the median density of the thyroglobulin molecules before and after endocytosis was only evident for the equilibrium‐labelled, normally iodinated rat preparation: the disappearence from the medium of 25‐ 30% of exogenous iodoproteins was sufficient to lower significantly the median density of the remaining molecules. This means that the thyroglobulin molecules having higher density are taken up preferentially by the tissue. A mechanism involving specific interactions between the iodoproteins and the surFace of thyroid cell is suggested.