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...

Sulfur Assimilation

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...

Lifecycle of Erythrocytes

Lifecycle of Erythrocytes

Erythrocytes, also known as red blood cells, constantly move through blood capillaries. As a result, they damage their plasma membrane due to the continuous friction. Typically, after 100 to 120 days, erythrocytes become rigid and fragile as they wear out. As they pass through small vessels in the spleen and liver, they can get trapped and break apart into fragments.
The resident phagocytic macrophages deal with these damaged cells by engulfing them and separating their globin and heme groups.

Nuclear Export

Nuclear Export

The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...

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,...

Erythropoiesis

Erythropoiesis

Red blood cells (RBCs) transport oxygen to all body tissues. These cells survive only for 120 days and then need to be replenished. Erythropoiesis is the process of RBC production. In healthy individuals, erythropoiesis ensures all tissues are amply supplied with oxygen. In addition, blood loss due to injury leads to a drop in the physiological oxygen level that will cause erythropoiesis. Any defect in erythropoiesis leads to several physiological disorders, including thalassemia, anemia, and...

You might also read

Related Articles

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

Sort by

Same author

Improving Pharmacokinetics of PSMA/GRPR-Targeting Radiolabeled Heterodimer through Enhanced Albumin Binding.

Molecular pharmaceutics·2026

Same author

Bithiophene Scaffold for PET Imaging and Photosensitization as a Novel Theranostic Platform Targeting Amyloid-β Aggregates.

ACS chemical neuroscience·2026

Same author

Systematic Investigation of Fatty Acids with Different Carbon-Chain Length as Albumin Binder to Improve Tumor Accumulation of Radioligands.

Bioconjugate chemistry·2026

Same author

Head-to-Head Comparison of Monomeric, Homodimeric, and Heterodimeric Fibroblast Activation Protein-Targeting Radioligands Based on Small Molecule Inhibitor and Cyclic Peptide.

ACS pharmacology & translational science·2026

Same author

Development of Novel Cholecystokinin 2 Receptor-Targeted Radioligand Containing Albumin Binder for Efficient <sup>111</sup>In/<sup>177</sup>Lu Theranostics.

Bioconjugate chemistry·2026

Same author

Engagement of the TCR against an oncolytic virus generates a population of effector CAR T cells with potent antitumor activity.

Science advances·2026

Search research articles

Related Experiment Video

Updated: Jul 8, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Hemoglobin-mediated selenium export from red blood cells.

Mamoru Haratake¹, Katsuyoshi Fujimoto, Ritsuko Hirakawa

¹Graduate School of Biomedical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, 852-8521, Japan. haratake@nagasaki-u.ac.jp

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry

|January 5, 2008

Summary

Hemoglobin (Hb) facilitates selenium export from red blood cells (RBCs) by transferring bound selenium to membrane proteins. This process is oxygen-dependent, with deoxygenated Hb promoting faster selenium release.

More Related Videos

Biological Samples Preparation for Speciation at Cryogenic Temperature using High-Resolution X-Ray Absorption Spectroscopy

Biological Samples Preparation for Speciation at Cryogenic Temperature using High-Resolution X-Ray Absorption Spectroscopy

Published on: May 27, 2022

Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay

Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay

Published on: January 31, 2022

Related Experiment Videos

Last Updated: Jul 8, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Biological Samples Preparation for Speciation at Cryogenic Temperature using High-Resolution X-Ray Absorption Spectroscopy

Biological Samples Preparation for Speciation at Cryogenic Temperature using High-Resolution X-Ray Absorption Spectroscopy

Published on: May 27, 2022

Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay

Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay

Published on: January 31, 2022

Area of Science:

Biochemistry
Cell Biology
Environmental Health

Background:

Selenium is an essential trace element, and its transport out of red blood cells (RBCs) is not fully understood.
Selenite is known to bind to hemoglobin (Hb), suggesting a potential role for Hb in selenium metabolism within RBCs.

Purpose of the Study:

To investigate the mechanism of selenium export from RBCs, focusing on the transfer of selenium from Hb to RBC membrane proteins.
To elucidate the molecular interactions involved in Hb-mediated selenium transport across the RBC membrane.

Main Methods:

Synthesized a hemoglobin-selenium (Hb-Se) complex as a model.
Examined the interaction of the Hb-Se complex with RBC inside-out vesicles (IOVs).
Utilized chemical inhibition (iodoacetamide) and enzymatic digestion (alpha-chymotrypsin) to identify protein involvement.

Main Results:

Selenium transferred from Hb to IOV membranes, binding to the cytoplasmic domains of band 3 protein (CDB3).
Selenium transfer was mediated by Hb interacting with thiol groups on CDB3.
Deoxygenated Hb showed higher affinity for CDB3 and facilitated more efficient selenium transfer compared to oxygenated Hb.
In vivo studies showed increased selenium export from RBCs under conditions favoring deoxygenated Hb.

Conclusions:

Hemoglobin plays a role in the export of selenium from red blood cells.
The selenium export process is linked to hemoglobin's oxygenation state, with deoxygenation promoting transfer.
This suggests an oxygen-linked mechanism for selenium efflux from RBCs mediated by hemoglobin.