@article{3047614,
    title = "HB ARTA [BETA-45 (CD4) PHE-]CYS] - A NEW UNSTABLE HEMOGLOBIN WITH
REDUCED OXYGEN-AFFINITY IN TRANS WITH BETA-THALASSEMIA",
    author = "VASSILOPOULOS, G and PAPASSOTIRIOU, I and VOSKARIDOU, E and and STAMOULAKATOU, A and PREMETIS, E and KISTER, J and MARDEN, M and and GRIFFON, N and POYART, C and WAJCMAN, H and GALACTEROS, F and and LOUKOPOULOS, D",
    journal = "British Journal of Haematology",
    year = "1995",
    volume = "91",
    number = "3",
    pages = "595-601",
    publisher = "Wiley",
    issn = "0007-1048, 1365-2141",
    doi = "10.1111/j.1365-2141.1995.tb05353.x",
    keywords = "HB VARIANT; UNSTABLE HB; LOW OXYGEN AFFINITY; BETA-DEGREES-THALASSEMIA",
    abstract = "The interaction of rare Hb variants with beta degrees-thalassaemia
results in a quasihomozygous state where the erythrocytes contain the
variant as the only major adult Hb component, Such a situation is a
unique model that enables functional studies even in the case of a
neutral variant that could not be isolated from Hb A, We report here an
unusual patient carrying Hb Arta, a novel Hb variant [beta 45 (CD4)
Phe –> Cys], in trans with beta degrees-thalassaemia gene (beta degrees
39). The aminoacid substitution at the critical CD corner of this Hb
molecule renders the molecule unstable. In addition, haem is displaced
in a position that favours the deoxy (T) conformation of the variant,
but less than in Hb Cheverly [beta 45 (CD4) Phe –> Ser], and results
in a p50 of 43 mmHg (pH 7.4, 37 degrees C) in the red cells with
preservation of cooperativity. Solution studies of the almost pure Hb
Arta show a 50% decrease in oxygen affinity and normal cooperativity;
the Bohr effect and the interaction with organic phosphates are similar
to those of Hb A. Hb Arta retains both normal homo- and heterotropic
effects allowing a well-preserved oxygen transport in vivo despite a
mild anaemia."
}