Iron release from transferrin

Synergistic interaction between adenosine triphosphate and an ammonium sulfate fraction of hemolysate

Simeon Pollack, Janet Weaver

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

In previous work we have shown that red cell hemolysates, at neutral pH, will release iron from transferrin; with molecular sieve chromatography, that activity separated into low molecular weight and high molecular weight components, both susceptible to destruction by phosphatases. Thus the possibility that nucleotides might be involved was suggested. We have studied the interaction of adenosine triphosphate (ATP) and an ammonium sulfate fraction of hemolysate with transferrin. ATP, as well as adenosine diphosphate and 2,3-diphosphoglyceric acid, interacts synergistically with the ammonium sulfate hemolysate fraction to promote iron release from transferrin. This activity is not limited to phosphorylated compounds, because citrate shows a similar effect. This activity is not a nonspecific chelating effect, because deferoxamine is without activity. All the synergistic anions labilize transferrin's HCO3. We therefore suggest that they form a non-HCO3 ternary complex with transferrin and iron, and that release of iron from this complex is promoted by a high molecular weight constituent of the hemolysate.

Original languageEnglish (US)
Pages (from-to)406-410
Number of pages5
JournalThe Journal of Laboratory and Clinical Medicine
Volume108
Issue number5
StatePublished - 1986

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Ammonium Sulfate
Transferrin
Iron
Adenosine Triphosphate
Molecular Weight
Molecular weight
2,3-Diphosphoglycerate
Deferoxamine
Molecular sieves
Chelation
Chromatography
Phosphoric Monoester Hydrolases
Citric Acid
Adenosine Diphosphate
Gel Chromatography
Anions
Nucleotides
Cells

ASJC Scopus subject areas

  • Medicine(all)
  • Pathology and Forensic Medicine

Cite this

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title = "Iron release from transferrin: Synergistic interaction between adenosine triphosphate and an ammonium sulfate fraction of hemolysate",
abstract = "In previous work we have shown that red cell hemolysates, at neutral pH, will release iron from transferrin; with molecular sieve chromatography, that activity separated into low molecular weight and high molecular weight components, both susceptible to destruction by phosphatases. Thus the possibility that nucleotides might be involved was suggested. We have studied the interaction of adenosine triphosphate (ATP) and an ammonium sulfate fraction of hemolysate with transferrin. ATP, as well as adenosine diphosphate and 2,3-diphosphoglyceric acid, interacts synergistically with the ammonium sulfate hemolysate fraction to promote iron release from transferrin. This activity is not limited to phosphorylated compounds, because citrate shows a similar effect. This activity is not a nonspecific chelating effect, because deferoxamine is without activity. All the synergistic anions labilize transferrin's HCO3. We therefore suggest that they form a non-HCO3 ternary complex with transferrin and iron, and that release of iron from this complex is promoted by a high molecular weight constituent of the hemolysate.",
author = "Simeon Pollack and Janet Weaver",
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TY - JOUR

T1 - Iron release from transferrin

T2 - Synergistic interaction between adenosine triphosphate and an ammonium sulfate fraction of hemolysate

AU - Pollack, Simeon

AU - Weaver, Janet

PY - 1986

Y1 - 1986

N2 - In previous work we have shown that red cell hemolysates, at neutral pH, will release iron from transferrin; with molecular sieve chromatography, that activity separated into low molecular weight and high molecular weight components, both susceptible to destruction by phosphatases. Thus the possibility that nucleotides might be involved was suggested. We have studied the interaction of adenosine triphosphate (ATP) and an ammonium sulfate fraction of hemolysate with transferrin. ATP, as well as adenosine diphosphate and 2,3-diphosphoglyceric acid, interacts synergistically with the ammonium sulfate hemolysate fraction to promote iron release from transferrin. This activity is not limited to phosphorylated compounds, because citrate shows a similar effect. This activity is not a nonspecific chelating effect, because deferoxamine is without activity. All the synergistic anions labilize transferrin's HCO3. We therefore suggest that they form a non-HCO3 ternary complex with transferrin and iron, and that release of iron from this complex is promoted by a high molecular weight constituent of the hemolysate.

AB - In previous work we have shown that red cell hemolysates, at neutral pH, will release iron from transferrin; with molecular sieve chromatography, that activity separated into low molecular weight and high molecular weight components, both susceptible to destruction by phosphatases. Thus the possibility that nucleotides might be involved was suggested. We have studied the interaction of adenosine triphosphate (ATP) and an ammonium sulfate fraction of hemolysate with transferrin. ATP, as well as adenosine diphosphate and 2,3-diphosphoglyceric acid, interacts synergistically with the ammonium sulfate hemolysate fraction to promote iron release from transferrin. This activity is not limited to phosphorylated compounds, because citrate shows a similar effect. This activity is not a nonspecific chelating effect, because deferoxamine is without activity. All the synergistic anions labilize transferrin's HCO3. We therefore suggest that they form a non-HCO3 ternary complex with transferrin and iron, and that release of iron from this complex is promoted by a high molecular weight constituent of the hemolysate.

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