Identification of abnormal hemoglobin from human blood

Published August 19, 2019

"Hb AC" denotes heterozygous β-chains: one normal, and one with a single mutation of glutamic acid to lysine at amino acid sequence position 6.

Precise determination of hemoglobin sequence and subunit quantitation from human blood for diagnosis of hemoglobin-based diseases.

What did scientists discover?

Human hemoglobin is a protein responsible for oxygen transport in the blood. It consists of two "alpha" and two "beta" subunits. Researchers have identified more than 1,500 structurally abnormal hemoglobins in human patients, some of which cause debilitating diseases, including sickle cell disease, which afflicts millions of people throughout the world.

There is currently no rapid way to confidently identify unknown hemoglobin variants. However, a collaboration of MagLab users recently reported a comprehensive, fast, and accurate characterization of hemoglobin for clinical diagnosis of human blood by using the unique capabilities of the MagLab's 21T Fourier Transform ‒ Ion Cyclotron Resonance (FT ‒ ICR) mass spectrometer.

Why is this important?

The method has successfully identified variants in hemoglobin in a few minutes, including a newly-discovered variant, thereby holding promise to provide clinicians with a valuable new tool for personalized medicine.

Who did the research?

L. He¹, A. L. Rockwood^2,3, A. M. Agarwal^3,4, L. C. Anderson⁵, C. R. Weisbrod⁵, C. L. Hendrickson^1,5, A. G. Marshall^1,5

¹Department of Chemistry and Biochemistry, Florida State University; ²Rockwood Scientific Consulting; ³University of Utah Health; ⁴ARUP Institute for Clinical and Experimental Pathology; ⁵Ion Cyclotron Resonance Program, National MagLab

Why did they need the MagLab?

This analysis requires ultrahigh mass resolving power and mass accuracy to confidently identify the hemoglobin amino acid sequences, a feat which is best accomplished by the MagLab's 21 tesla FT ‒ ICR mass spectrometer.