title: Recombinant H-chain ferritins: effects of changes in the 3-fold channels.
abstract: Human H-chain ferritins bearing sequence changes in the 3-fold channels have been expressed in E. coli to investigate the role of these channels in iron-storage processes. The proteins assemble into shells resembling those of native ferritins. Iron uptake measurements indicate that residues in the 3-fold channels are involved neither in initial Fe(II)-oxidation nor in iron-core nucleation.
authors.affiliation: Department of Molecular Biology and Biotechnology, The University, Sheffield, England.
authors.forename: A
authors.initials: A
authors.lastname: Treffry
authors.forename: P M
authors.initials: PM
authors.lastname: Harrison
authors.forename: A
authors.initials: A
authors.lastname: Luzzago
authors.forename: G
authors.initials: G
authors.lastname: Cesareni
mesh_terms: D000595:Amino Acid Sequence; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D005293:Ferritins / Q000378:metabolism*; D006801:Humans; D007501:Iron / Q000378:metabolism; D009154:Mutation; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013329:Structure-Activity Relationship
chemical_list: D011994:Recombinant Proteins; D005293:Ferritins; D007501:Iron