Hb-Alberta or α2β2(101(G3) GLU→GLY), a New High-Oxygen-Affinity Hemoglobin Variant Causing Erythrocytosis

Autor:	Nancy Cope, M. E. Gravely, M. L. Salkie, Titus H.J. Huisman, M. Jayalakshmi, Francine Appling, Kathleen Bolch, J. B. Wilson, M. J. Mant
Rok vydání:	1976
Předmět:	Chemistry Stereochemistry education Biochemistry (medical) Clinical Biochemistry Subunit interaction Heterozygote advantage Bohr effect Hematology Oxygen affinity Residue (chemistry) Hb Alberta Genetics (clinical) High-oxygen-affinity hemoglobin
Zdroj:	Hemoglobin. 1:183-194
ISSN:	1532-432X 0363-0269
DOI:	10.3109/03630267608991679
Popis:	Hb-Alberta has been found in a 51 year old Caucasian male with erythrocytosis. The substitution in this variant involves the glutamyl residue in position lOl(G3) of the β chain which is replaced by a glycyl residue. Hb-Alberta accounts for about 45% in the heterozygote, and readily forms hybrid tetramers with other hemoglobins. The oxygen affinity of Hb-Alberta is greatly increased, its Bohr effect reduced, and its subunit interaction greatly diminished.
Databáze:	OpenAIRE
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