Evidence that H-enriched human placental ferritin is structurally similar to L-enriched ferritins of other tissues.

Academic Article

Abstract

  • Ferritin was purified from normal full-term placenta, and the native structure and subunit composition were characterized. Reversed-phase high-performance liquid chromatographic analysis of the placental ferritin subunits suggested the presence of three subunit types. Using acid urea gel electrophoresis and amino acid analysis, these subunits were tentatively identified as two H-type and one L-type. The relative proportions of the subunit types were approx. 23% H-1, 33% H-2 and 44% L. The native structure of placental ferritin as judged by circular dichroism and fluorescence spectroscopy was quite similar to that of ferritin isolated from horse spleen, a source that is composed predominantly of L subunits. These results are consistent with a ferritin tetracosameric structure whose H and L subunits fit into 24 equivalent sites interchangeably because the secondary and tertiary structures of the two subunit types are very similar.
  • Keywords

  • Amino Acids, Apoferritins, Chromatography, High Pressure Liquid, Circular Dichroism, Electrophoresis, Polyacrylamide Gel, Female, Ferritins, Humans, Macromolecular Substances, Placenta, Pregnancy, Terbium
  • Digital Object Identifier (doi)

    Author List

  • Collawn JF; Donato H; Fish WW
  • Start Page

  • 235
  • End Page

  • 242
  • Volume

  • 871
  • Issue

  • 3