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Original Articles

Identification of a new hemoglobin variant Hb Liuzhou [HBA1:C.182A→G] by MALDI-TOF mass spectrometry during HbA1c measurement

ORCID Icon, , &
Pages 479-483 | Received 26 Apr 2020, Accepted 14 Jun 2020, Published online: 28 Jun 2020
 

Abstract

Structural hemoglobin (Hb) variant is generally caused by a point mutation in the globin gene that produces one amino acid substitution. Here, we describe a new α-chain variant found during HbA1c measurement. HbA1c procedures based on both ion-exchange high-performance liquid chromatography (HPLC) and capillary electrophoresis (CE) techniques failed to identify its presence. In contrast, MALDI-TOF mass spectrometry (MS) revealed the existence of a variant α-chain with a mass of 15155 Da. In addition, the Hb variant interfered with HbA1c determined by Bio-Rad D100. DNA sequencing confirmed the occurrence of a new heterozygous mutation [HBA1:C.182A→G] at codon 60, resulting in a coding change from lysine to arginine. We named it Hb Liuzhou for thde birthplace of the patient. This case exemplified that MALDI-TOF mass spectrometry can serve as the method of choice to identify and quantify the Hb variant.

Disclosure statement

No potential conflict of interest was reported by the author(s).

Additional information

Funding

This work was supported by Peking University Shenzhen Hospital under Grant [JCYJ2018005].

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