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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...
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,...
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...
Effect of Hepatic Disease on Pharmacokinetics: Pathophysiologic Assessment and Liver Function Test01:22

Effect of Hepatic Disease on Pharmacokinetics: Pathophysiologic Assessment and Liver Function Test

In clinical practice, the direct measurement of hepatic blood flow to evaluate liver function presents significant challenges due to the intricate and specialized nature of the necessary techniques. Consequently, healthcare professionals often rely on empirical estimates derived from thorough patient examinations and liver function tests to gauge liver health. Among the tools at their disposal, the Child–Pugh and MELD scoring systems stand out for their ability to categorize and assess the...
Factors Affecting Protein-Drug Binding: Patient-Related Factors01:29

Factors Affecting Protein-Drug Binding: Patient-Related Factors

Protein-drug binding, a pivotal aspect of pharmacokinetics, is subject to considerable variability influenced by an array of patient-related factors. The intricate interplay of age, individual differences, and pathological conditions significantly impact the binding dynamics and subsequent pharmacological effects.
Age stands as a key determinant in protein-drug binding. Neonates, characterized by low albumin content, experience heightened concentrations of unbound drugs such as phenytoin and...
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...

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Related Experiment Video

Updated: Jun 21, 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: basic and clinical aspects.

Andrew P Levy1, Rabea Asleh, Shany Blum

  • 1Department of Anatomy and Cell Biology, Rappaport Faculty of Medicine, Technion Israel Institute of Technology, Haifa, Israel. alevy@tx.technion.ac.il

Antioxidants & Redox Signaling
|August 8, 2009
PubMed
Summary
This summary is machine-generated.

Haptoglobin (Hp) genotype Hp 2-2 may increase diabetes complications. High-dose antioxidants could be a targeted therapy for Hp 2-2 diabetes mellitus patients.

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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

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Last Updated: Jun 21, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous &beta;2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

Area of Science:

  • Biochemistry
  • Genetics
  • Pharmacogenomics

Background:

  • Haptoglobin (Hp) is a plasma protein binding free hemoglobin.
  • Hp determines hemoglobin fate after red blood cell hemolysis.
  • Two common Hp alleles (1 and 2) exist with functional differences.

Purpose of the Study:

  • To investigate the clinical significance of haptoglobin functional differences.
  • To assess the risk of microvascular and macrovascular complications in Hp 2-2 individuals with diabetes mellitus (DM).

Main Methods:

  • Analysis of haptoglobin genetic locus and protein products.
  • Evaluation of clinical significance of Hp 1 vs. Hp 2 functional differences.
  • Assessment of risk in Hp 2-2 DM patients.

Main Results:

  • Hp 2-2 genotype shows functional differences in protecting against oxidative stress.
  • Hp 2-2 individuals with diabetes mellitus face significantly higher risks of complications.
  • Potential for pharmacogenomic intervention in this patient group.

Conclusions:

  • Haptoglobin genotype influences diabetes complication risk.
  • Hp 2-2 DM patients may benefit from targeted antioxidant therapy.
  • Pharmacogenomics offers a personalized treatment strategy for diabetes complications.