ArticlePloS one2013
Haptoglobin preferentially binds β but not α subunits cross-linked hemoglobin tetramers with minimal effects on ligand and redox reactions.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- Biophysical and Biochemical Characterization of High Molecular Weight Co-Polymerized Human Hemoglobin and Albumin as a Potential Hemoglobin-Based Oxygen Carrier.ACS biomaterials science & engineering · 2026Article
- Haptoglobin Genotypes in Hidradenitis Suppurativa: Haptoglobin 2-2 Genotype Is Associated With Familial Hidradenitis Suppurativa and More Flares.International journal of dermatology · 2025Article
- Poor Clearance of Free Hemoglobin Due to Lower Active Haptoglobin Availability is Associated with Osteoarthritis Inflammation.Journal of inflammation research · 2021Article
- Apohemoglobin-haptoglobin complexes attenuate the hypertensive response to low-molecular-weight polymerized hemoglobin.Blood advances · 2020Article
- Mechanisms of Toxicity and Modulation of Hemoglobin-based Oxygen Carriers.Shock (Augusta, Ga.) · 2019Review
- Hemoglobin-Based Blood Substitutes and the Treatment of Sickle Cell Disease: More Harm than Help?Biomolecules · 2017Review
- Oxidized Ferric and Ferryl Forms of Hemoglobin Trigger Mitochondrial Dysfunction and Injury in Alveolar Type I Cells.American journal of respiratory cell and molecular biology · 2016Article
- Haptoglobin attenuates hemoglobin-induced heme oxygenase-1 in renal proximal tubule cells and kidneys of a mouse model of sickle cell disease.Blood cells, molecules & diseases · 2015Article
- Redox properties of human hemoglobin in complex with fractionated dimeric and polymeric human haptoglobin.Free radical biology & medicine · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Human hemoglobin (Hb) and haptoglobin (Hp) exhibit an extremely high affinity for each other, and the dissociation of Hb tetramers into dimers is generally believed to be a prerequisite for complex formation. We have investigated Hp interactions with native Hb, αα, and ββ cross-linked Hb (ααXLHb and ββXLHb, respectively), and rapid kinetics of Hb ligand binding as well as the redox reactivity in the presence of and absence of Hp. The quaternary conformation of ββ subunit cross-linking results in a higher binding affinity than that of αα subunit cross-linked Hb. However, ββ cross-linked Hb exhibits a four fold slower association rate constant than the reaction rate of unmodified Hb with Hp. The Hp contact regions in the Hb dimer interfaces appear to be more readily exposed in ββXLHb than ααXLHb. In addition, apart from the functional changes caused by chemical modifications, Hp binding does not induce appreciable effects on the ligand binding and redox reactions of ββXLHb. Our findings may therefore be relevant to the design of safer Hb-based oxygen therapeutics by utilizing this preferential binding of ββXLHb to Hp. This may ultimately provide a safe oxidative inactivation and clearance pathway for chemically modified Hbs in circulation.
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