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Hemoglobin01:24

Hemoglobin

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Conjugated Proteins02:50

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
Protein Families02:47

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key locations, protein...
Globular Proteins01:27

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...

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Related Experiment Video

Updated: Jun 6, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Haptoglobin: old protein with new functions.

Abdu I Alayash1

  • 1Laboratory of Biochemistry and Vascular Biology, Division of Hematology, Center for Biologics Evaluation and Research, US Food and Drug Administration, Bethesda, MD 20892, USA. abdu.alayash@fda.hhs.gov

Clinica Chimica Acta; International Journal of Clinical Chemistry
|December 17, 2010
PubMed
Summary

Haptoglobin (Hp) protects against toxic free hemoglobin (Hb) by shielding key amino acids and preventing radical damage. This natural detoxification mechanism may be crucial for developing Hb-based oxygen therapeutics.

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Area of Science:

  • Biochemistry
  • Physiology
  • Toxicology

Background:

  • Free hemoglobin (Hb) released from red blood cells (RBCs) is toxic due to its heme center's redox activity.
  • Haptoglobin (Hp) is a natural protective mechanism that binds Hb subunits for safe degradation by macrophages.
  • Oxidative stress exacerbates Hb toxicity, necessitating understanding of protective interactions.

Purpose of the Study:

  • To investigate the protective mechanisms of haptoglobin (Hp) against free hemoglobin (Hb) toxicity under oxidative conditions.
  • To elucidate how Hp shields Hb and mitigates heme-induced oxidative damage.
  • To assess the therapeutic potential of Hb-Hp complexes in preventing Hb-related pathologies.

Main Methods:

  • Studied the interaction between Hb and Hp under oxidative stress.
  • Analyzed the shielding of specific amino acids on Hb by Hp.
  • Evaluated the effect of Hb-Hp complex infusion in animal models of Hb-induced injury.

Main Results:

  • Hp effectively shields critical amino acids on Hb, preventing damaging radical formation.
  • The Hb-Hp complex consumes oxidants and short-circuits damaging radicals.
  • Animal studies demonstrated that Hb-Hp infusion prevents Hb-induced hypertension and tissue injury.

Conclusions:

  • Haptoglobin (Hp) plays a vital role in detoxifying free hemoglobin (Hb) by modulating its redox activity.
  • Understanding Hb-Hp interactions offers potential strategies for mitigating Hb toxicity in clinical settings.
  • Hb-Hp complexes show promise for use in oxygen therapeutics and managing RBC storage lesions.