Assembly of intra- and interspecies hybrid apoferritins.
An intraspecies hybrid apoferritin was assembled by mixing subunits of horse heart ferritin, which consists mainly of H-type subunits, and horse spleen ferritin, in which L-type subunits predominate. Interspecies hybrid apoferritins were reconstituted from subunits of human liver-horse spleen ferritins and from rat liver-horse spleen ferritins. All the hybrid ferritins migrated as single zones with electrophoretic mobilities intermediate between those of the parent ferritins. Isoelectric focusing data and immunological patterns were consistent with the view that the reassembled apoferritins were composite molecules that contained subunits from each of the interacting forms. Reconstitution occurred in a random manner, as there was no apparent preference for assembly of homologous subunits. These results suggest that intersubunit interaction domains and recognition mechanisms that dictate formation of the highly specific quaternary structure assumed by this protein are common for different species of ferritins.
D000818:Animals; D001052:Apoferritins / Q000096:biosynthesis* / Q000276:immunology; D005293:Ferritins / Q000031:analogs & derivatives* / Q000378:metabolism; D006321:Heart; D006736:Horses; D006801:Humans; D006824:Hybridization, Genetic; D005779:Immunodiffusion; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism; D011489:Protein Denaturation; D051381:Rats; D013045:Species Specificity; D013154:Spleen / Q000378:metabolism
D005293:Ferritins; D001052:Apoferritins