We have previously shown that a subpopulation of cord/fetal red blood cells (RBC) binds rabbit IgG antibodies raised against cord RBC and absorbed on adult RBC (F-IgG), while control IgG, raised against and absorbed on adult RBC (A-IgG), fails to do so. In the present study, F-IgG maintained its binding to cord RBC surface antigens following absorption on spectrin but not after absorption on skeleton-stripped RBC membranes. Spectrin-absorbed F-IgG- but not A-IgG-affinity-purified material from cord RBC contained polypeptides with apparent MW of complement receptor 1 (CR1) allotypes. Moreover, on immunoblotting these polypeptides reacted with 125I-F-IgG as well as with 125I-anti-CR1 mAb, and binding of 125I-anti-CR1 mAb was inhibited by unlabelled F-IgG. In addition, cord RBC incubated with F-IgG prior to reaction with anti-CR1 showed decreased fluorescence intensity on flow cytometry. Taken together the results suggest that F-IgG binds to CR1 which shows increased expression/accessibility on a subpopulation of cord/fetal RBC.