Identification of hemoglobin G-Philadelphia (alpha 68 Asn replaced by Lys) and hemoglobin Matsue-Oki (alpha 75 Asp replaced by Asn) in a black infant.
Biochim Biophys Acta
; 707(2): 206-12, 1982 Oct 05.
Article
em En
| MEDLINE
| ID: mdl-6814490
ABSTRACT
Two alpha-chain variants, Hb G-Philadelphia and Hb Matsue-Oki, were present in members of a relatively large black family from South Carolina. The four Hb G-Philadelphia heterozygotes averaged 35.6% Hb G, suggesting the presence of an alpha-thalassemia-2 condition in cis to the Hb G mutation, which was confirmed by DNA structural analysis. The seven Hb Matsue-Oki heterozygotes averaged 22.2% Hb MO and likely have four active alpha-chain genes. One infant was a compound heterozygote for the two Hb variants which could not be separated from each other. The quantity of Hb G plus Hb MO was 58% by DEAE-cellulose chromatography and 69% by chain analyses. These results and the family data indicate that this child had three active alpha-chain genes, of which one regulated the synthesis of the normal alpha chain, one was mutated to give the alpha G chain, and one to give the alpha MO chain. The amino acid substitutions in Hb G-Philadelphia and Hb Matsue-Oki are located in the tryptic peptide alpha T-9, which is 29 amino acid residues long. Structural analyses of these abnormalities made use of high-pressure liquid chromatography for the separation of both tryptic and thermolytic peptides and of a highly sensitive ultra-micro sequencing procedure. Although the alpha 68 Asn replaced by Lys substitution is readily demonstrable in Hb G-Philadelphia the elucidation of the alpha 75 Asp replaced by Asn replacement in Hb Matsue-Oki was greatly facilitated by the use of these microprocedures.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Asparagina
/
Talassemia
/
Hemoglobinas Anormais
/
Ácido Aspártico
/
Lisina
Tipo de estudo:
Diagnostic_studies
/
Prognostic_studies
Limite:
Adolescent
/
Adult
/
Child
/
Female
/
Humans
/
Infant
/
Male
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1982
Tipo de documento:
Article