title: Functional assembly of recombinant human ferritin subunits in Pichia pastoris.
abstract: 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.
authors.affiliation: Department of Food Science, Massachusetts Agricultural Experiment Station, University of Massachusetts, Amherst, MA 01003, USA.
authors.forename: Jung-Lim
authors.initials: JL
authors.lastname: Lee
authors.forename: Cheon-Seok
authors.initials: CS
authors.lastname: Park
authors.forename: Hae-Yeong
authors.initials: HY
authors.lastname: Kim
mesh_terms: D001052:Apoferritins; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D005293:Ferritins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D006801:Humans; D007501:Iron / Q000378:metabolism; D046529:Microscopy, Electron, Transmission; D008970:Molecular Weight; D010088:Oxidoreductases; D010843:Pichia / Q000235:genetics*; D010957:Plasmids; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
chemical_list: C507433:FTL protein, human; D011994:Recombinant Proteins; D005293:Ferritins; D001052:Apoferritins; D007501:Iron; C454461:FTH1 protein, human; D010088:Oxidoreductases