Lin Zhichao, Lin Qing, Zhu Feng, Huang Heqing
Department of Biochemistry and Biotechnology, School of Life Sciences, Xiamen University, Xiamen 361005, China.
Se Pu. 2009 Jan;27(1):96-101.
The pancreas ferritins from chickens, ducks, cattle and pigs were isolated by thermal denaturation, ammonium sulphate fractionation and DEAE-52 cellulose anion exchange chromatography separately, in order to obtain the characteristics both subunit types and isoelectric points. Four ferritins such as chicken pancreas ferritin (ChPF), duck pancreas ferritin (DPF), cattle pancreas ferritin (CaPF), and pig pancreas ferritin (PPF) showed different mobility in polyacrylamide gel electrophoresis (PAGE). The relative molecular masses (M(r)) of these ferritin were indicated to be M(r) (ChPF) > M(r) (DPF) > M(r) (CaPF) > M(r) (PPF), which are all bigger than that in horse spleen ferritin (HSF). Sodium dodecyl sulfate (SDS)-PAGE results indicate that ChPF, DPF, CaPF and PPF consist of H and L subunits, showing different ratios of H/L subunits. Two subunit types in the ferritin were further identified by peptide-mass fingerprinting (PMF) technology. The four ferritins such as ChPF, DPF, CaPF and PPF in denatured-isoelectric focusing (IEF) gel show the subunit polymers containing from 3 to 6 with different pI values, respectively. These phenomena reveal the complicated interactions and different polymers between H and L subunits in the ferritins. There are differences both interaction intensities and polymers in the ferritin subunits coming from different mammals. These heterogeneity may response to the rate of iron release in ferritins and to the detoxification requirement of iron in animals in vivo.
分别通过热变性、硫酸铵分级分离和DEAE - 52纤维素阴离子交换色谱法分离鸡、鸭、牛和猪的胰腺铁蛋白，以获得亚基类型和等电点的特征。鸡胰腺铁蛋白（ChPF）、鸭胰腺铁蛋白（DPF）、牛胰腺铁蛋白（CaPF）和猪胰腺铁蛋白（PPF）这四种铁蛋白在聚丙烯酰胺凝胶电泳（PAGE）中表现出不同的迁移率。这些铁蛋白的相对分子质量（M(r)）显示为M(r)（ChPF）> M(r)（DPF）> M(r)（CaPF）> M(r)（PPF），均大于马脾铁蛋白（HSF）的相对分子质量。十二烷基硫酸钠（SDS）-PAGE结果表明，ChPF、DPF、CaPF和PPF由H和L亚基组成，显示出不同的H/L亚基比例。通过肽质量指纹图谱（PMF）技术进一步鉴定了铁蛋白中的两种亚基类型。变性等电聚焦（IEF）凝胶中的ChPF、DPF、CaPF和PPF这四种铁蛋白分别显示出含有3至6个不同pI值的亚基聚合物。这些现象揭示了铁蛋白中H和L亚基之间复杂的相互作用和不同的聚合物。来自不同哺乳动物的铁蛋白亚基在相互作用强度和聚合物方面存在差异。这些异质性可能与铁蛋白中铁的释放速率以及动物体内铁的解毒需求有关。
