Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Hemoglobin

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 Blood

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,...

Carbon Dioxide Transport in the Blood

Carbon Dioxide Transport in the Blood

Carbon dioxide (CO2) transport in the blood is critical to human physiology. On average, our body cells produce around 200 mL of CO2 per minute, precisely the quantity expelled by the lungs. This process involves the transportation of CO2 from the tissue cells to the lungs in three primary forms.
Forms of CO2 Transport
1. Dissolved in plasma: A small percentage (7-10%) of CO2 is transported and dissolved directly in the plasma.
2. Carbaminohemoglobin: Just over 20% of CO2 is chemically bound to...

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...

Hypoxia

Hypoxia

Hypoxia is a medical condition characterized by an inadequate oxygen supply to body tissues. It typically manifests as a bluish discoloration of the skin and mucosae, especially in fair-skinned individuals, when hemoglobin (Hb) saturation drops below 75%.
Types of Hypoxia
There are four primary types of hypoxia, each resulting from a different cause:
1. Anemic hypoxia: This type occurs due to insufficient oxygen delivery caused by a lack of red blood cells (RBCs) or RBCs with abnormal or...

Treatment for Pulmonary Arterial Hypertension: Oxygen Therapy for Respiratory Failure

Treatment for Pulmonary Arterial Hypertension: Oxygen Therapy for Respiratory Failure

Oxygen therapy has emerged as a significant tool in enhancing the quality of life for patients suffering from pulmonary arterial hypertension (PAH). While this therapy has principally been studied on patients with significant hypoxemia, this therapeutic approach helps prevent potential organ damage and can be administered in the comfort of one's home.
Oxygen therapy is vital in increasing and maintaining blood oxygen levels in PAH patients. As a result, it aids in reducing fatigue,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Modulation of O<sub>2</sub> Affinity and Enzymatic Activity of Core‒Shell Structured Hemoglobin Nanoparticles.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same author

A reappraisal of APOE genetic effects on Alzheimer's disease risk in the Japanese population: a meta-analysis.

Molecular neurodegeneration·2026

Same author

Incorporating Euglena gracilis into the habitual diet modulates immune function and reduces common cold-like symptoms: a randomized controlled trial.

Nutrition journal·2026

Same author

Mass spectrometry-based proteomic profiling of human tauopathy brains suggests mitochondria-associated alterations.

Frontiers in molecular neuroscience·2026

Same author

Multidisciplinary Trends in Endoscopic Surgery in Japan: Insights From the 17th Nationwide Survey.

Asian journal of endoscopic surgery·2026

Same author

Bioavailability of Functional Iron in Protein Microparticles.

Nutrients·2026

Search research articles

Related Experiment Video

Updated: Aug 20, 2025

Author Spotlight: Utilizing Next-Generation Polymerized Human Hemoglobin for Improved Donor Lung Evaluation and Preservation in Rats

Author Spotlight: Utilizing Next-Generation Polymerized Human Hemoglobin for Improved Donor Lung Evaluation and Preservation in Rats

Published on: June 14, 2024

Core-Shell Structured Hemoglobin Nanoparticles as Artificial O₂ Carriers.

Wataru Okamoto¹, Mai Hasegawa¹, Natsumi Kohyama¹

¹Department of Applied Chemistry, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga, Bunkyo-ku, Tokyo 112-8551, Japan.

ACS Applied Bio Materials

|November 18, 2022

Summary

Researchers developed novel hemoglobin nanoparticles (HbNPs) as artificial oxygen carriers and potential red blood cell substitutes. These HbNPs demonstrate promising oxygen binding properties and improved circulation longevity for diverse medical applications.

Keywords:

O2 binding blood compatibility catalase circulation lifetime human serum albumin recombinant hemoglobin red blood cell substitute stroma-free hemoglobin

More Related Videos

Encapsulating Cytochrome c in Silica Aerogel Nanoarchitectures without Metal Nanoparticles while Retaining Gas-phase Bioactivity

Encapsulating Cytochrome c in Silica Aerogel Nanoarchitectures without Metal Nanoparticles while Retaining Gas-phase Bioactivity

Published on: March 1, 2016

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

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

Published on: December 7, 2016

Related Experiment Videos

Last Updated: Aug 20, 2025

Author Spotlight: Utilizing Next-Generation Polymerized Human Hemoglobin for Improved Donor Lung Evaluation and Preservation in Rats

Author Spotlight: Utilizing Next-Generation Polymerized Human Hemoglobin for Improved Donor Lung Evaluation and Preservation in Rats

Published on: June 14, 2024

Encapsulating Cytochrome c in Silica Aerogel Nanoarchitectures without Metal Nanoparticles while Retaining Gas-phase Bioactivity

Encapsulating Cytochrome c in Silica Aerogel Nanoarchitectures without Metal Nanoparticles while Retaining Gas-phase Bioactivity

Published on: March 1, 2016

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

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

Published on: December 7, 2016

Area of Science:

Biomaterials Science
Nanotechnology
Biochemistry

Background:

Development of effective red blood cell (RBC) substitutes is crucial for transfusion medicine.
Hemoglobin (Hb) nanoparticles (NPs) offer potential as artificial oxygen carriers.

Purpose of the Study:

To synthesize and characterize core-shell structured hemoglobin nanoparticles (HbNPs).
To evaluate the oxygen (O₂) binding properties and potential of HbNPs as RBC substitutes.

Main Methods:

Polymerization of human adult Hb using specific chemical crosslinkers to form parent particles.
Covalent wrapping of parent particles with human serum albumin (HSA) to create 100 nm HbNPs.
Fabrication of entirely synthetic particles using recombinant Hb and HSA, including variants.
Incorporation of catalase into stroma-free Hb (SFHb) to create SFHbNPs.

Main Results:

HbNPs exhibited higher O₂ affinity than native RBCs, though NPs under N₂ showed reduced affinity.
Recombinant Hb variant NPs displayed slightly lower O₂ affinity.
SFHbNPs with catalase formed stable O₂ complexes, showed good blood compatibility, and had longer circulation half-lives in rats compared to naked Hb.

Conclusions:

Hb-based NPs are viable alternative materials for RBC substitutes.
SFHbNPs demonstrate potential as effective O₂ therapeutic reagents for various medical scenarios.