Hb Sitia [beta 128(H6)Ala -> Val]: An unstable variant with a substitutionin the alpha 1 beta 1 interface

Authors
Papassotiriou, I Traeger-Synodinos, J Prome, D Kister, J Vrettou, C Xaidara, A Marden, M Stamoulakatou, A Wajcman, H Kanavakis, E
Citation
I. Papassotiriou et al., Hb Sitia [beta 128(H6)Ala -> Val]: An unstable variant with a substitutionin the alpha 1 beta 1 interface, HEMOGLOBIN, 25(1), 2001, pp. 45-56
Citations number
19
Categorie Soggetti
Biochemistry & Biophysics
Journal title
HEMOGLOBIN
ISSN journal
03630269 → ACNP
Volume
25
Issue
1
Year of publication
2001
Pages
45 - 56
Database
ISI
SICI code
0363-0269(2001)25:1<45:HS[1-V>2.0.ZU;2-J
Abstract
Hb Sitia [beta 128(H6)Ala --> Val] was found in a Greek female with slightl y reduced red blood cell indices. The abnormal hemoglobin was indistinguish able from Wb A by electrophoresis but eluted after Hb A on cation exchange high performance liquid chromatography. DNA sequence analysis revealed a GC T --> GTT mutation at codon 128, which is predicted to encode an Ala --> Va l substitution. This was confirmed by mass spectrometry analyses of the bet a -globin chain. Since alanine at beta 128(H6) interacts with several amino acids of the alpha1 beta1 contact, its replacement by a larger residue res ults in a mild instability of the molecule and slight modifications of the oxygen binding properties.