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

被引：0

作者：

TURPEINEN, U

SIPILA, I

ANTTILA, P

KARJALAINEN, U

KURONEN, B

KALKKINEN, N

AHOLA, T

STENMAN, UH

机构：

[1] AURORA HOSP,SF-00250 HELSINKI,FINLAND

[2] MARIA HOSP,SF-00180 HELSINKI,FINLAND

[3] MALMI HOSP,SF-00780 HELSINKI,FINLAND

[4] UNIV HELSINKI,INST BIOTECHNOL,SF-00380 HELSINKI,FINLAND

[5] TAMPERE UNIV HOSP,SF-33521 TAMPERE,FINLAND

来源：

CLINICAL CHEMISTRY | 1995年 / 41卷 / 04期

关键词：

GLYCOHEMOGLOBIN; CHROMATOGRAPHY; REVERSED-PHASE; AMINO ACID SEQUENCING;

D O I：

暂无

中图分类号：

R446 [实验室诊断]; R-33 [实验医学、医学实验];

学科分类号：

1001 ;

摘要：

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 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].

引用

页码：532 / 536

页数：5