Clinical Chemistry
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Clinical Chemistry 41: 532-536, 1995;
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Clinical Chemistry, Vol 41, 532-536, Copyright © 1995 by American Association for Clinical Chemistry

Two alpha-chain hemoglobin variants, Hb Broussais and Hb Cemenelum, characterized by cation-exchange HPLC, isoelectric focusing, and peptide sequencing

U Turpeinen, I Sipila, P Anttila, U Karjalainen, B Kuronen, N Kalkkinen, T Ahola and UH Stenman
Helsinki University Central Hospital, Finland.

We here report the characteristics of two rare alpha-chain hemoglobin (Hb) variants. The variants were found during quantification of HbA1c by cation-exchange HPLC with the Diamat glycohemoglobin analyzer. They were further characterized by isoelectric focusing and PolyCAT A cation- exchange chromatography. The structure of the abnormal Hbs was established by amino acid analysis after separation of the globin chains by reversed-phase chromatography, digestion with trypsin, separation of the peptides by reversed-phase chromatography, and amino acid sequencing. These studies showed that the two variants were Hb Broussais [alpha 90 (FG2)Lys-->Asn] and Hb Cemenelum [alpha 92 (FG4)Arg- ->Trp].


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 Clin. Chem.Home page
G. M. Clarke and T. N. Higgins
Laboratory Investigation of Hemoglobinopathies and Thalassemias: Review and Update
Clin. Chem., August 1, 2000; 46(8): 1284 - 1290.
[Abstract] [Full Text] [PDF]


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