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

Search research articles

Related Experiment Videos

Some properties of hemoglobin A2

H M Ranney¹, R Lam, G Rosenberg

¹Department of Medicine, Veterans Affairs Medical Center, University of California, San Diego.

American Journal of Hematology

|January 1, 1993

Summary

Hemoglobin A2 (Hb A2) shows increased susceptibility to oxidation and lower solubility compared to Hemoglobin A. These properties, along with more stable denaturation products, may explain Hb A2's greater binding to red cell membranes.

Related Concept Videos

You might also read

Related Articles

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

Sort by

Same author

Utility of stool culture for the diagnosis and management of paediatric TB in a low-burden setting.

IJTLD open·2026

Same author

Investigating the 'liquid-solid interface' in the comprehensive genomic profiling of metastatic colorectal cancer for guiding treatment-where do we draw the line?

Annals of oncology : official journal of the European Society for Medical Oncology·2024

Same author

A Six-year-old Girl With a Non-tender Cheek Swelling.

Clinical infectious diseases : an official publication of the Infectious Diseases Society of America·2023

Same author

A Variable Neighbourhood Descent Heuristic for Conformational Search Using a Quantum Annealer.

Scientific reports·2019

Same author

Virus Genotype-Dependent Transcriptional Alterations in Lipid Metabolism and Inflammation Pathways in the Hepatitis C Virus-infected Liver.

Scientific reports·2019

Same author

Surgical management of a cat with hepatic arterioportal fistula.

The Journal of small animal practice·2018

Area of Science:

Biochemistry
Hematology
Cell Biology

Background:

Hemoglobin A2 (Hb A2) is a minor component of human hemoglobin with an unrecognized physiologic function.
Hb A2 and its oxidative denaturation product, hemichrome A2, bind more strongly to red cell membranes (band 3) than Hemoglobin A (Hb A) and hemichrome A.
Understanding Hb A2 properties is crucial for elucidating its role in hemoglobin-membrane interactions.

Purpose of the Study:

To investigate the biochemical properties of Hb A2 that may influence its association with the red cell membrane.
To compare the oxidative stability, solubility, and denaturation products of Hb A2 with Hb A.

Main Methods:

Comparative analysis of autoxidation rates of Hb A2 and Hb A to methemoglobin.
Assessment of enzymatic reduction rates and heme-globin linkage stability for methemoglobins A and A2.
Determination of oxyhemoglobin A2 solubility in phosphate buffer.
Spectroscopic and stability analysis of hemichromes A2 and A prepared using phenylhydrazine.

Main Results:

Hb A2 demonstrated slightly increased susceptibility to autoxidation, forming methemoglobin A2.
No significant differences were observed in the enzymatic reduction rates or heme-globin linkage stability between methemoglobins A and A2.
Oxyhemoglobin A2 exhibited slightly lower solubility in phosphate buffer compared to oxyhemoglobin A.
While hemichromes A2 and A shared similar optical spectra, hemichrome A2 showed enhanced stability.

Conclusions:

The observed differences in oxidative denaturation products, particularly the greater stability of hemichrome A2, may underlie the differential binding of Hb A2 to red cell membranes.
These findings suggest potential functional implications of Hb A2 beyond its established role in oxygen transport.
Further research into Hb A2's interactions with cellular components is warranted.

Related Experiment Videos