title: Purification of fusion ferritin from recombinant E. coli using two-step sonications.
abstract: Fusion ferritin, combined by heavy chain ferritin (21 kDa) and light chain ferritin (19 kDa), was expressed in recombinant E. coli. The fusion ferritin was easily purified by two-step sonications as well as gel filtration chromatography. SDS-gel electrophoresis showed a single band of 38 kDa with heavy and light chains. MALDI-TOF MS gave a molecular weight of fusion ferritin was 38 kDa. The specific activity and yield of purified fusion ferritin are 0.41 Fe3+ mg mg(-1) of protein and 66%. Those values are larger than the previous ones of 0.2 Fe3+ mg mg(-1) (Kim et al. 2001).
authors.affiliation: Department of Chemical Engineering, Chungnam National University, 220 Gung-Dong, Yusong-gu, Daejeon, 305-764, Korea.
authors.forename: Yun Suk
authors.initials: YS
authors.lastname: Huh
authors.forename: In Ho
authors.initials: IH
authors.lastname: Kim
mesh_terms: D004926:Escherichia coli / Q000145:classification / Q000302:isolation & purification / Q000378:metabolism* / Q000528:radiation effects*; D005293:Ferritins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D008970:Molecular Weight; D010865:Pilot Projects; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification; D013010:Sonication; D013045:Species Specificity
chemical_list: D011993:Recombinant Fusion Proteins; D005293:Ferritins