Specific binding of placental acidic isoferritin to cells of the T-cell line HD-MAR

A. M. Konijn, E. G. Meyron-Holtz, R. Levy, H. Ben-Bassat, Y. Matzner

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


Acidic placental isoferritin inhibited the blastogenic response of peripheral human lymphocytes to T-cell activating lectins. We measured specific binding of radioiodinated placental isoferritin to cells of the T-cell line HD-MAR and found specific high-affinity binding. Binding was faster and more ferritin was bound at 37°C than at 4°C. Displacement experiments indicated that most of the binding occurred at the cell surface. Acidic placental ferritin and isolated H-type ferritin subunits but not isolated L-type subunits, competed for the binding. Scatchard plot analysis showed characteristics of a single binding species with a dissociation constant (Kd) of 1.3-4.4 × 10-11 M. The results suggest the presence of receptors for acidic isoferritin on T-lymphocytes and thus, a regulatory role for the acidic ferritin H-type subunit in T-cell function.

Original languageEnglish
Pages (from-to)229-232
Number of pages4
JournalFEBS Letters
Issue number2
StatePublished - 24 Apr 1990
Externally publishedYes


  • Ferritin
  • Isoferritin
  • Receptor
  • T-cell

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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