Two alpha-chain hemoglobin variants, Hb Broussais and Hb Cemenelum, characterized by cation-exchange HPLC, isoelectric focusing, and peptide sequencing.
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].
Turpeinen
U
U
Helsinki University Central Hospital, Finland.
Sipilä
I
I
Anttila
P
P
Karjalainen
U
U
Kuronen
B
B
Kalkkinen
N
N
Ahola
T
T
Stenman
U H
UH
D000293:Adolescent; D000595:Amino Acid Sequence; D002412:Cations; D002648:Child; D002851:Chromatography, High Pressure Liquid; D005260:Female; D005914:Globins / Q000737:chemistry* / Q000235:genetics; D006442:Glycated Hemoglobin / Q000032:analysis; D006455:Hemoglobins, Abnormal / Q000737:chemistry*; D006801:Humans; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D008297:Male; D008969:Molecular Sequence Data; D009154:Mutation; D012016:Reference Values; D017421:Sequence Analysis
D002412:Cations; D005914:Globins; D006442:Glycated Hemoglobin; D006455:Hemoglobins, Abnormal; C093169:hemoglobin Broussais; C086688:hemoglobin Cemenelum