ArticleFree radical biology & medicine2014
Redox properties of human hemoglobin in complex with fractionated dimeric and polymeric human haptoglobin.
Article in Free radical biology & medicine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 2 of them syntheses that pooled it.
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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
42 citing papers in PubMed, 2 syntheses or guidelines pooled it, 62 citations in OpenAlex.
- Haptoglobin genotype and aneurysmal subarachnoid hemorrhage: Individual patient data analysis.Neurology · 2019Pooled it
- Haptoglobin Genotype and Outcome after Subarachnoid Haemorrhage: New Insights from a Meta-Analysis.Oxidative medicine and cellular longevity · 2017Pooled it
- Evaluation of the Methemoglobin-Haptoglobin Protein Complex for Detoxification of Cyanide, Azide, and Sulfide in In Vitro Binding Models.Chemical research in toxicology · 2026Article
- Cryo-EM provides insight into how thebioRxiv : the preprint server for biology · 2026Article
- Hemoglobin-based oxygen carriers: Biochemical, biophysical differences, and safety.Transfusion · 2025Article
- Molecular basis of hemoglobin binding and heme removal inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Protein dynamics govern the oxyferrous state lifetime of an artificial oxygen transport protein.Biophysical journal · 2023Article
- The Shr receptor fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Ultraviolet light oxidation of fresh hemoglobin eliminates aggregate formation seen in commercially sourced hemoglobin.Blood cells, molecules & diseases · 2023Article
- GOx/Hb Cascade Oxidized Crosslinking of Silk Fibroin for Tissue-Responsive Wound Repair.Gels (Basel, Switzerland) · 2022Article
- Hemoglobin can Act as a (Pseudo)-PeroxidaseFrontiers in molecular biosciences · 2022Article
- βCysteine 93 in human hemoglobin: a gateway to oxidative stability in health and disease.Laboratory investigation; a journal of technical methods and pathology · 2021Review
- Kinetics of cyanide and carbon monoxide dissociation from ferrous human haptoglobin:hemoglobin(II) complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Apohemoglobin-haptoglobin complex attenuates the pathobiology of circulating acellular hemoglobin and heme.American journal of physiology. Heart and circulatory physiology · 2020Article
- The Interplay between Molten Globules and Heme Disassociation Defines Human Hemoglobin Disassembly.Biophysical journal · 2020Article
- Lessons Learned from 50 Years of Hemoglobin Research: Unstirred and Cell-Free Layers, Electrostatics, Baseball Gloves, and Molten Globules.Antioxidants & redox signaling · 2020Review
- The Chemical Basis of Intracerebral Hemorrhage and Cell Toxicity With Contributions From Eryptosis and Ferroptosis.Frontiers in cellular neuroscience · 2020Article
- Mechanisms of haemolysis-induced kidney injury.Nature reviews. Nephrology · 2019Review
- Mechanisms of Toxicity and Modulation of Hemoglobin-based Oxygen Carriers.Shock (Augusta, Ga.) · 2019Review
- Current Challenges in the Development of Acellular Hemoglobin Oxygen Carriers by Protein Engineering.Shock (Augusta, Ga.) · 2019Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Haptoglobin (Hp) is an abundant and conserved plasma glycoprotein, which binds acellular adult hemoglobin (Hb) dimers with high affinity and facilitates their rapid clearance from circulation after hemolysis. Humans possess three main phenotypes of Hp, designated Hp 1-1, Hp 2-1, and Hp 2-2. These variants exhibit diverse structural configurations and have been reported to be functionally nonequivalent. We have investigated the functional and redox properties of Hb-Hp complexes prepared using commercially fractionated Hp and found that all forms exhibit similar behavior. The rate of Hb dimer binding to Hp occurs with bimolecular rate constants of ~0.9 μM(-1) s(-1), irrespective of the type of Hp assayed. Although Hp binding does accelerate the observed rate of HbO2 autoxidation by dissociating Hb tetramers into dimers, the rate observed for these bound dimers is three- to fourfold slower than that of Hb dimers free in solution. Co-incubation of ferric Hb with any form of Hp inhibits heme loss to below detectable levels. Intrinsic redox potentials (E1/2) of the ferric/ferrous pair of each Hb-Hp complex are similar, varying from +54 to +59 mV (vs NHE), and are essentially the same as reported by us previously for Hb-Hp complexes prepared from unfractionated Hp. All Hb-Hp complexes generate similar high amounts of ferryl Hb after exposure to hydrogen peroxide. Electron paramagnetic resonance data indicate that the yields of protein-based radicals during this process are approximately 4 to 5% and are unaffected by the variant of Hp assayed. These data indicate that the Hp fractions examined are equivalent to one another with respect to Hb binding and associated stability and redox properties and that this result should be taken into account in the design of phenotype-specific Hp therapeutics aimed at countering Hb-mediated vascular disease.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.