Lee Jung-Lim, Park Cheon-Seok, Kim Hae-Yeong
Department of Food Science, Massachusetts Agricultural Experiment Station, University of Massachusetts, Amherst, MA 01003, USA.
J Microbiol Biotechnol. 2007 Oct;17(10):1695-9.
Ferritin is an iron storage protein found in most living organisms as a natural assembled macromolecule. For studying the functional ability of the ferritin assembly, human H- and L-ferritins were expressed and purified from Pichia pastoris strain GS115. The recombinant H- and L-ferritins showed a globular form with transmission electron microscopy. The rate of iron uptake for H-ferritin was significantly faster than that for the L-ferritin in vitro. By gel permeation chromatography analysis, recombinant ferritins were confirmed as multimeric subunits with high molecular weight and it was indicated that assembled subunits were able to store iron in vivo.
铁蛋白是一种铁储存蛋白，作为一种天然组装的大分子存在于大多数生物体内。为了研究铁蛋白组装体的功能能力，从毕赤酵母菌株GS115中表达并纯化了人H型和L型铁蛋白。重组H型和L型铁蛋白在透射电子显微镜下呈球状。在体外，H型铁蛋白的铁摄取速率明显快于L型铁蛋白。通过凝胶渗透色谱分析，证实重组铁蛋白为高分子量的多聚体亚基，表明组装后的亚基能够在体内储存铁。
