Recombinant H-chain ferritins: effects of changes in the 3-fold channels

FEBS Lett. 1989 Apr 24;247(2):268-72. doi: 10.1016/0014-5793(89)81350-x.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallization
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme-Linked Immunosorbent Assay
  • Ferritins / metabolism*
  • Humans
  • Iron / metabolism
  • Mutation
  • Protein Conformation
  • Recombinant Proteins / metabolism*
  • Spectrophotometry, Ultraviolet
  • Structure-Activity Relationship

Substances

  • Recombinant Proteins
  • Ferritins
  • Iron