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Cited by 601Iron Metabolism and DisordersHemoglobin structure and functionProtein Interaction Studies and Fluorescence Analysis

Stoichiometric and site characteristics of the binding of iron to human transferrin

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Aisen, P., Leibman, A., Zweier, J.·1978·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)62337-9
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  • Transferrin is a glycoprotein containing two high affinity binding sites for ferric iron, which captures Fe3+ in the circulation.

    “Transferrin (Tf) is a glycoprotein containing two high affinity binding sites for ferric iron (Fe3+) (Aisen et al., 1978), which captures Fe3+ in the circulation (Figure 1).”

    From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Aisen et al., 1978

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References 27 · Cited by 601

Authors
Aisen, P., Leibman, A., & Zweier, J.
Affiliations
Yeshiva University (US)
ORCID
Zweier, J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1978-03
Volume
253
Issue
6
Pages
1930-1937
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(19)62337-9
OpenAlex
W1551307287
Cited by
601
References
27
Citations by year
2026: 3 · 2025: 11 · 2024: 15 · 2023: 20 · 2022: 17 · 2021: 17 · 2020: 15 · 2019: 22 · 2018: 17 · 2017: 25 · 2016: 13 · 2015: 14 · 2014: 19 · 2013: 18 · 2012: 18
FWCI
9.49
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Keywords
transferrin, iron binding, binding sites, iron transport, protein-ligand binding
MeSH terms
Binding Sites, Electron Spin Resonance Spectroscopy, Humans, Iron, Kinetics, Protein Binding, Protein Conformation, Thermodynamics, Transferrin

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