Purification of fusion ferritin from recombinant E. coli using two-step sonications.
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).
Huh
Yun Suk
YS
Department of Chemical Engineering, Chungnam National University, 220 Gung-Dong, Yusong-gu, Daejeon, 305-764, Korea.
Kim
In Ho
IH
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
D011993:Recombinant Fusion Proteins; D005293:Ferritins