Otsuka S, Listowsky I, Niitsu Y, Urushizaki I
J Biol Chem. 1980 Jul 10;255(13):6234-7.
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.
通过混合马心铁蛋白（主要由H型亚基组成）和马脾铁蛋白（L型亚基占主导）的亚基，组装出了一种种内杂交脱铁铁蛋白。从人肝 - 马脾铁蛋白亚基以及大鼠肝 - 马脾铁蛋白亚基中重构出了种间杂交脱铁铁蛋白。所有杂交铁蛋白在电泳中均迁移为单一区带，其电泳迁移率介于亲本铁蛋白之间。等电聚焦数据和免疫模式与以下观点一致：重新组装的脱铁铁蛋白是复合分子，包含来自每种相互作用形式的亚基。重构以随机方式发生，因为对于同源亚基的组装没有明显偏好。这些结果表明，决定该蛋白假定的高度特异性四级结构形成的亚基间相互作用结构域和识别机制在不同种类的铁蛋白中是常见的。
