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Related Concept Videos

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...
Drug Distribution: Plasma Protein Binding01:29

Drug Distribution: Plasma Protein Binding

Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
Drug Binding to Blood Components01:30

Drug Binding to Blood Components

When drugs enter systemic circulation, they interact with various components of the blood, including proteins such as human serum albumin (HSA), α1-acid glycoprotein (AAG), lipoproteins, globulins, and red blood cells (RBCs).
HSA is the most abundant plasma protein and is vital in drug binding. It contains distinct drug-binding sites, with different drugs exhibiting affinity for specific sites. There are three main drug-binding domains for HSA: sites I, II, and III. These domains are further...
Oxygen Transport in the Blood01:27

Oxygen Transport in the Blood

Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...
Blood Typing01:10

Blood Typing

Understanding an individual's blood group is a critical component of transfusion medicine. It ensures compatibility in blood transfusions, organ transplants, and even during pregnancy. Determining these blood groups involves the ABO and Rh blood typing systems, utilizing specific antigens and corresponding anti-sera to identify an individual's blood type.
Antigens are protein molecules that reside on the surface of red blood cells (RBCs). The ABO and Rh blood typing systems target antigens A,...
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...

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Updated: Jun 4, 2026

A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering
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A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering

Published on: December 7, 2016

Identification of plasma haptoglobin forms which loosely bind hemoglobin.

Maria Stefania Spagnuolo1, Luisa Cigliano, Bernardetta Maresca

  • 1Istituto per il Sistema Produzione Animale in Ambiente Mediterraneo, Consiglio Nazionale delle Ricerche, Naples, Italy.

Biological Chemistry
|February 8, 2011
PubMed
Summary

Haptoglobin (Hpt) exhibits two forms of hemoglobin (Hb) binding. Increased levels of loosely bound Hpt (LB-Hpt) in acute coronary syndrome patients suggest altered Hpt functions and potential disease associations.

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A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering
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A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering

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Iridium(III) Luminescent Probe for Detection of the Malarial Protein Biomarker Histidine Rich Protein-II
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Iridium(III) Luminescent Probe for Detection of the Malarial Protein Biomarker Histidine Rich Protein-II

Published on: July 7, 2015

Area of Science:

  • Biochemistry
  • Cardiovascular Science
  • Proteomics

Background:

  • Haptoglobin (Hpt) is a plasma protein crucial for scavenging free hemoglobin (Hb).
  • Hpt interacts with apolipoproteins (Apo) A-I and E, influencing lipid metabolism.
  • The functional implications of different Hpt-Hb binding affinities remain incompletely understood.

Purpose of the Study:

  • To characterize distinct forms of Haptoglobin-hemoglobin complexes.
  • To investigate the association of these forms with acute coronary syndrome (ACS).
  • To evaluate the functional consequences of altered Hpt-Hb binding on apolipoprotein interactions.

Main Methods:

  • Differential ultracentrifugation to separate tightly bound Hpt (TB-Hpt) and loosely bound Hpt (LB-Hpt) from Hb.
  • Quantification of TB-Hpt and LB-Hpt in patient cohorts using biochemical assays.
  • Assessment of ApoA-I and ApoE binding affinities to Hpt forms via co-immunoprecipitation.
  • Enzyme activity assays for lecithin-cholesterol acyltransferase (LCAT).
  • Analysis of post-translational modifications, including nitrotyrosine and glycan profiling.

Main Results:

  • Haptoglobin binds hemoglobin in two distinct states: tightly bound (TB-Hpt, ~80%) and loosely bound (LB-Hpt, ~20%).
  • LB-Hpt levels were significantly elevated (>60%) in patients with acute coronary syndrome.
  • LB-Hpt exhibited reduced binding affinity for ApoA-I (8-fold less) and ApoE (4-fold less) compared to TB-Hpt.
  • Neither Hpt form altered the LCAT-stimulating activity of ApoA-I.
  • While nitrotyrosine levels were comparable, distinct glycan profiles were observed between LB-Hpt and TB-Hpt.

Conclusions:

  • The existence of distinct Hpt-Hb binding states suggests differential functional roles.
  • Elevated LB-Hpt in ACS patients indicates a potential link between altered Hpt-Hb complex formation and cardiovascular disease.
  • Reduced apolipoprotein binding by LB-Hpt may have implications for lipid metabolism and reverse cholesterol transport in disease states.