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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 101(G3) of the beta 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.
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Mant et al. (1976) studied this question.
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