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Electrospray mass spectrometric characterization of hemoglobin Q (Hb Q-India) and a double mutant hemoglobin S/D in clinical samples.

Abstract：

OBJECTIVES:The clinical analysis of hemoglobin by ion exchange chromatography can result in ambiguities in identification of the nature of the globin chain present in patient samples. LC/ESI-MS provides rapid and precise determination of globin chain masses. DESIGN AND METHODS:Hemolysate of hemoglobin Q-India and hemoglobin S/D/F have been analyzed using ESI-MS. Tandem-MS has been used to establish mutation in alpha chain of hemoglobin Q. RESULTS:The identification of hemoglobin Q-India is readily achieved by LC/ESI-MS, which establishes the presence of a mutant alpha chain differing in mass from normal alpha chain by 22 Da. The site of mutation has been identified by tandem-MS analysis of a tryptic fragment encompassing residues alphaV62-K90. LC/ESI-MS screening has also provide an example of simultaneous occurrence of mutant globin chains containing beta6E-->V (Hb S, sickle) and beta121E-->Q (Hb D) variant. Expression of gamma(G) globin chain is also demonstrated in this sample. CONCLUSIONS:The site of mutation in hemoglobin Q-India is identified as alpha64D-->H which differs from mutations alpha74D-->H in Hb Q-Thailand and alpha75D-->H in Hb Q-Iran. Mass spectrometric analysis of hemoglobins from a patient and her parents suggests inheritance of mutant beta globin genes from both parents.

journal_name

Clin Biochem

journal_title

Clinical biochemistry

authors

Mandal AK,Bisht S,Bhat VS,Krishnaswamy PR,Balaram P

doi

10.1016/j.clinbiochem.2007.09.006

subject

Has Abstract

pub_date

2008-01-01 00:00:00

pages

75-81

issue

1-2

eissn

0009-9120

issn

1873-2933

pii

S0009-9120(07)00362-1

journal_volume

41

pub_type

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