Identification of a new hemoglobin variant Hb Liuzhou [HBA1:C.182A→G] by MALDI-TOF mass spectrometry during HbA1c measurement. (1st October 2020)

• Record Type: Journal Article
• Authors: Xu, Anping; Chen, Weidong; Xie, Weijie; Ji, Ling
• Is Part Of: Scandinavian journal of clinical & laboratory investigation. Volume 80:Number 6(2020)
• Page Start: 479
• Page End: 483
• Publication Date: 2020-10-01
• Subjects: Hemoglobin variant -- MALDI-TOF mass spectrometry -- HbA1c -- HBA1:C.182A→G -- Hb Liuzhou; Clinical biochemistry -- Periodicals; Physiology, Pathological -- Periodicals; Physiology, Experimental -- Periodicals; Medicine -- Research -- Periodicals; Clinical medicine -- Periodicals; 616.0072
• DOI: 10.1080/00365513.2020.1783698
• Languages: English
• ISSNs: 0036-5513

Abstract

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.