Online citations, reference lists, and bibliographies.

Separation Of Hemoglobin Variants By Capillary Electrophoresis.

F. Cotton, B. Gulbis
Published 2013 · Chemistry, Medicine

Cite This
Download PDF
Analyze on Scholarcy
Share
Quantitative defects in hemoglobin (Hb) are represented by Hb variants, where the amino acids sequence is modified as a consequence of a mutation in the α or β-globin genes. More than 1,100 variants have been described so far but only a few dozen are clinically significant; the most significant being Hb S, which in the homozygous state causes sickle cell disease. The majority of the methods used to detect Hb variants are based on the charge difference of the mutated globin chain. We have developed a micellar capillary electrophoresis (MEKC) method using highly acidic conditions and a high Triton(®) concentration. Separation times in the order of 20 min were able to resolve all normal and 29 abnormal globin chains including Hb E. This method was initially developed for Beckman P/ACE 5500 Instrument but has been modified for the more recent P/ACE MDQ and PA 800 instruments; however, the method can be adapted to any kind of CE analyzer.
This paper references
10.1016/0021-9673(92)87128-U
Capillary electrophoresis of hemoglobins and globin chains.
M. Zhu (1992)
Evaluation of an automated capillary electrophoresis system in the screening for hemoglobinopathies.
Frédéric Cotton (2009)
10.1093/CLINCHEM/46.8.1284
Laboratory investigation of hemoglobinopathies and thalassemias: review and update.
G. Clarke (2000)
10.1016/S0009-8981(99)00167-9
Capillary isoelectric focusing of haemoglobin variants in the clinical laboratory.
M. Jenkins (1999)
10.1258/000456303770367261
The place of capillary electrophoresis techniques in screening for haemoglobinopathies
B. Gulbis (2003)
Diagnostic biologique des hémoglobinopathies par analyse du phénotype
V. Siguret (1997)
10.1093/CLINCHEM/43.11.2137
Capillary isoelectric focusing and high-performance cation-exchange chromatography compared for qualitative and quantitative analysis of hemoglobin variants.
N. Mario (1997)
10.1002/bmc.1130060504
Detection of abnormal haemoglobin by capillary electrophoresis and structural identification.
N. Ishioka (1992)
10.1002/elps.1150181013
Capillary isoelectric focusing of hemoglobin variants in the pediatric clinical laboratory
J. Hempe (1997)
10.3109/03630269908996155
Capillary zone electrophoresis: an additional technique for the identification of hemoglobin variants.
C. Lin (1999)
10.1126/science.6190229
Interaction of human hemoglobin and its variants with agar.
W. P. Winter (1983)
10.1002/elps.11501601246
Screening of umbilical cord blood hemoglobins by isoelectric focusing in capillaries
M. Conti (1995)
10.1515/CCLM.2006.059
Evaluation of a new Sebia kit for analysis of hemoglobin fractions and variants on the Capillarys® system
A. Louahabi (2006)
10.1016/S0950-3536(98)80074-7
6 Pathophysiology of sickle cell disease
M. Steinberg (1998)
Evaluation of hemoglobin A2 quantitation assay and hemoglobin variant screening by capillary electrophoresis.
M. Jenkins (1997)
10.1016/S0021-9673(01)90459-5
Reversed-phase high-performance liquid chromatography of human haemoglobin chains.
L. Leone (1985)
10.1093/ajcp/107.1.88
Hemoglobin A2 levels in healthy persons, sickle cell disease, sickle cell trait, and beta-thalassemia by capillary isoelectric focusing.
R. Craver (1997)
10.1081/HEM-100104026
ABNORMAL HEMOGLOBINS: LABORATORY METHODS
H. Wajcman (2001)
10.1093/clinchem/37.1.14
Capillary electrophoresis--a new clinical tool.
F. T. Chen (1991)
10.1016/j.clinbiochem.2010.06.009
Newborn screening for hemoglobinopathies using capillary electrophoresis technology: Testing the Capillarys Neonat Fast Hb device.
Eleni Mantikou (2010)
10.1093/CLINCHEM/45.2.237
Evaluation of a capillary electrophoresis method for routine determination of hemoglobins A2 and F.
F. Cotton (1999)
10.1016/S0378-4347(97)00444-1
Qualitative and quantitative analysis of hemoglobin variants by capillary isoelectric focusing.
N. Mario (1998)
10.1309/AJCPD0PJGFT0SXMK
Prevalence of elevated hemoglobin A2 measured by the CAPILLARYS system.
Zhaohai Yang (2009)
10.1016/S0950-3536(98)80072-3
4 Pathophysiology of thalassaemia
D. Weatherall (1998)
10.1016/j.clinbiochem.2009.01.004
Comparison of two methods for the quantification and identification of hemoglobin variants.
T. Higgins (2009)
10.1016/S0268-960X(02)00061-9
Screening and genetic diagnosis of haemoglobin disorders.
J. Old (2003)
10.1093/clinchem/43.4.644
Capillary electrophoresis system for hemoglobin A1c determinations evaluated.
C. Doelman (1997)
10.1002/(SICI)1522-2683(20000301)21:4<743::AID-ELPS743>3.0.CO;2-1
Separation of hemoglobin variants with similar charge by capillary isoelectric focusing: Value of isoelectric point for identification of common and uncommon hemoglobin variants
J. Hempe (2000)
10.1002/elps.1150150105
Application of dynamic capillary isoelectric focusing to the analysis of human hemoglobin variants
S. Molteni (1994)
ProteinHaemoglobin analysis by capillary zone electrophoresis
Ahmet Şahin (1995)
10.1093/clinchem/40.12.2288
Quantification of hemoglobin variants by capillary isoelectric focusing.
J. Hempe (1994)
10.1093/clinchem/45.8.1317
Interference of hemoglobin D in hemoglobin A(2) measurement by cation-exchange HPLC.
F. Cotton (1999)
10.1016/0021-9673(93)80652-O
Capillary electrophoresis of abnormal hemoglobins associated with α-thalassemias
M. Zhu (1993)
10.1002/ELPS.200410043
Simplified hemoglobin chain detection by capillary electrophoresis
Z. Shihabi (2005)
10.1016/0378-4347(92)80210-H
Separation of globins using free zone capillary electrophoresis.
C. Ong (1992)
Analysis of hemoglobin variants by capillary isoelectric focusing.
J. Hempe (1997)
10.1016/0021-9673(95)00229-G
Haemoglobin analysis by capillary zone electrophoresis
A. Sahin (1995)
10.1002/(SICI)1522-2683(20000301)21:4<749::AID-ELPS749>3.0.CO;2-E
Hemoglobin A2 quantification by capillary zone electrophoresis
Z. Shihabi (2000)
10.1016/S0378-4347(98)00418-6
Separation of human globin chains by micellar electrokinetic capillary chromatography.
C. Lin (1998)



This paper is referenced by
Semantic Scholar Logo Some data provided by SemanticScholar