Identification of a new hemoglobin variant Hb Liuzhou [HBA1:C.182A→G] by MALDI-TOF mass spectrometry during HbA1c measurement.
An-Ping XuWeidong ChenWeijie XieLing JiPublished in: Scandinavian journal of clinical and laboratory investigation (2020)
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.
Keyphrases
- mass spectrometry
- high performance liquid chromatography
- capillary electrophoresis
- liquid chromatography
- gas chromatography
- high resolution
- tandem mass spectrometry
- amino acid
- simultaneous determination
- ms ms
- case report
- nitric oxide
- risk assessment
- single cell
- solid phase extraction
- magnetic resonance imaging
- dna damage
- single molecule
- contrast enhanced
- circulating tumor
- transcription factor
- quantum dots
- energy transfer