Lee S S, Richter G W
Biochemistry. 1976 Jan 13;15(1):65-70. doi: 10.1021/bi00646a011.
We have reinvestigated the association and dissociation of ferritin and apoferritin in phosphate buffer (pH 7.2, I = 0.05). When oligomer-enriched solutions of horse spleen ferritin were mixed with more concentrated, but unenriched solutions of horse spleen apoferritin, there was dissociation of the ferritin oligomers, as determined by polyacrylamide gel electrophoresis and from iron/protein ratios. Some evidence was also obtained for association of monomers in the mixture of ferritin and apoferritin after pelleting and redissolution of pellets in minimal volumes of the phosphate buffer. Monomer-enriched, biosynthetically labeled rat liver ferritin was pelleted, redissolved in minimal volumes of phosphate buffer, and separated by polyacrylamide gel electrophoresis; the fractions were isolated and counted. The results revealed that an association of monomers of the rat liver ferritin had taken place which doubled the concentration of dimers. However, our results also indicate that association by concentration was limited to a fraction of monomers.
我们重新研究了铁蛋白和脱铁铁蛋白在磷酸盐缓冲液（pH 7.2，离子强度I = 0.05）中的缔合和解离情况。当将富含寡聚体的马脾铁蛋白溶液与浓度更高但未富集的马脾脱铁铁蛋白溶液混合时，通过聚丙烯酰胺凝胶电泳和铁/蛋白比率测定，发现铁蛋白寡聚体发生了解离。在将铁蛋白和脱铁铁蛋白混合物中的沉淀进行沉淀并在最小体积的磷酸盐缓冲液中重新溶解后，还获得了一些关于单体缔合的证据。将富含单体的、经生物合成标记的大鼠肝脏铁蛋白进行沉淀，在最小体积的磷酸盐缓冲液中重新溶解，然后通过聚丙烯酰胺凝胶电泳进行分离；对各组分进行分离并计数。结果显示，大鼠肝脏铁蛋白单体发生了缔合，使二聚体浓度增加了一倍。然而，我们的结果也表明，通过浓缩进行的缔合仅限于一部分单体。
