Characterization of a new electrophoretically silent hemoglobin variant -: Hb Saale OR α2β2 84(EF8)Thr → ala

被引：2

作者：

Bissé, E

Zorn, N

Heinrichs, I

Eigel, A

Van Dorsselaer, A

Wieland, H

Kister, J

Marden, MC

机构：

[1] Univ Hosp, Dept Clin Chem, D-79106 Freiburg, Germany

[2] Univ Strasbourg 1, Fac Chim, Lab Spectrometrie Masse Bioorgan, CNRS,URA 31, F-67008 Strasbourg, France

[3] Univ Munster, Inst Humangenet, D-48149 Munster, Germany

[4] INSERM, U473, F-94276 Le Kremlin Bicetre, France

[5] Univ Halle Wittenberg, Div Pediat, D-06097 Halle, Germany

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2000年 / 275卷 / 28期

关键词：

D O I：

10.1074/jbc.M001827200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A new abnormal hemoglobin was detected in a young German anemic patient by cation-exchange high performance liquid chromatography (HPLC), Using a combination of electrospray mass spectrometry, HPLC, direct sequencing, and family screening with polymerase chain reaction/restriction digestion approach, we have characterized this hemoglobin variant as resulting from a Thr --> Ala replacement at beta 84(EF8). It could be separated neither by electrophoresis nor by isoelectric focusing. Hb Saale is slightly unstable, exhibiting a moderate tendency to auto-oxidize. Functional properties and the heterotropic interactions are similar to those of Hb A.

引用

页码：21380 / 21384

页数：5

共 21 条

[1] HB F-BASKENT OR ALPHA-2A-GAMMA-128(H6)ALA-]THR [J].