An antiserum obtained from a sheep immunized with pooled sheep vitreous body was shown to contain allotypic antibodies which defined a specificity designated A. Subsequent immunization of 5 sheep with sheep sera elicited antibodies which recognized 7 additional allotypic specificities designated B, C, D, E, F, G and H. Comparison of antigenic specificities in double diffusion gel precipitation indicated that in sera containing allotypes C and E, C and H, or E and H, both allotypes were often expressed on the same molecule although subpopulations of molecules possessing only one of the specificities could also be demonstrated. Physicochemical tests characterized A and B as relatively small α-glycoproteins. Specificity A was apparently determined by carbohydrate while specificity B was manifested by the protein portion of a molecule rich in sialic acid. Specificities C, E and H appeared to be carried by α2-macroglobulin. Allotypes A, B, D, F and G were shown to be synthesized in utero while specificities C, E and H were not detected in fetuses. Transplacental crossing of allo-type-bearing components was not demonstrated. Inheritance of allotypes appeared to be under control of dominant autosomal genes. Convincing evidence for Mendelian dominant inheritance was presented on the basis of family studies for allotypes A, B and E. The occurrence of allotype combinations in the general population along with results of specific matings suggested that the inheritance of C, E and H may be determined by gene complexes.