The protein component of the iron storage molecule, ferritin, contains 24 subunits in form of a hollow shell known as apoferritin. The amino acid sequence has been determined for apoferritin subunits from human liver. The sequence comprises 174 amino acids giving an it4* of 19 900. It shows extensive homology with the primary structures of apoferritins from human and horse spleen and from rat Iiver. Sequence substitutions are discussed in relation to the known three-dimensional structure of horse spleen apoferritin.Evidence for a second minor sequence in human liver apoferritin is presented. Human liver upoferritin

Immunoreactivities of peptides purified after cleavage of human liver apoferritin are reported and discussed in relation to the known 3‐dimensional and primary structures of homologous apoferritins. These studies point to 3 antigenic sites occupying continuous inter‐helical regions of the polypeptide chains which lie on the surface of the apoferritin molecule. Other antigenic regions may encompass amino acids remote in the primary structure or belonging to different subunits.

No abstract