Partial characterization of transferrins of some species of the family Cyprinidae.

1. Transferrins of five cyprinid fishes (Tinca tinca, Ctenopharyngodon idella, Chondrostoma nasus. Hypophthalmichthys molitrix and Aristichthys nobilis) were isolated in a pure state using Sephadex G-100, DEAE-Sephadex and SP-Sephadex. 2. All the transferrins are heterogeneous. In H. molitrix and A. nobilis the heterogeneity is caused partly, but not exclusively, by the presence of sialic acid; in the other species it is independent of sialic acid. 3. Molecular weights ranging from 69,900 (T. tinca) to 78,800 (H. molitrix) were obtained by sedimentation equilibrium ultracentrifugation. SDS-polyacrylamide gel electrophoresis with beta-mercaptoethanol indicated that the transferrins are composed of a single polypeptide chain. 4. Amino acid compositions of all species were similar, the greatest similarity being in the transferrins of H. molitrix and A. nobilis. 5. Carbohydrate was not found in transferrins of T. tinca and C. idella, but was present in A. nobilis (2.63%) and H. molitrix (5.01%). 6. Alanine was N-terminal in C. idella. No N-terminal amino acid was found in T. tinca, H. molitrix and A. nobilis.