2 ALPHA-CHAIN HEMOGLOBIN-VARIANTS, HB-BROUSSAIS AND HB-CEMENELUM, CHARACTERIZED BY CATION-EXCHANGE HPLC, ISOELECTRIC-FOCUSING, AND PEPTIDE SEQUENCING

Authors
TURPEINEN U SIPILA I ANTTILA P KARJALAINEN U KURONEN B KALKKINEN N AHOLA T STENMAN UH
Citation
U. Turpeinen et al., 2 ALPHA-CHAIN HEMOGLOBIN-VARIANTS, HB-BROUSSAIS AND HB-CEMENELUM, CHARACTERIZED BY CATION-EXCHANGE HPLC, ISOELECTRIC-FOCUSING, AND PEPTIDE SEQUENCING, Clinical chemistry, 41(4), 1995, pp. 532-536
Citations number
19
Categorie Soggetti
Chemistry Medicinal
Journal title
Clinical chemistry → ACNP
ISSN journal
00099147
Volume
41
Issue
4
Year of publication
1995
Pages
532 - 536
Database
ISI
SICI code
0009-9147(1995)41:4<532:2AHHAH>2.0.ZU;2-4
Abstract
We here report the characteristics of two rare alpha-chain hemoglobin (Hb) variants. The variants were found during quantification of HbA(1c ) by cation-exchange HPLC with the Diamat(TM) glycohemoglobin analyzer . They were further characterized by isoelectric focusing and PolyCAT A cation-exchange chromatography. The structure of the abnormal Hbs wa s established by amino acid analysis after separation of the globin ch ains by reversed-phase chromatography, digestion with trypsin, separat ion of the peptides by reversed-phase chromatography, and amino acid s equencing. These studies showed that the two variants were Hb Broussai s [alpha 90 (FG2)Lys-->Asn] and Hb Cemenelum [alpha 92 (FG4)Arg-->Trp] .