Functional assembly of recombinant human ferritin subunits in Pichia pastoris.
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.
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
C507433:FTL protein, human; D011994:Recombinant Proteins; D005293:Ferritins; D001052:Apoferritins; D007501:Iron; C454461:FTH1 protein, human; D010088:Oxidoreductases