PDF] Hemoglobin polymorphism in white-tailed deer: subunit basis.
![PDF] Hemoglobin polymorphism in white-tailed deer: subunit basis.](https://d3i71xaburhd42.cloudfront.net/442de7651b90997b8b5c2ac0309ecaf101fed8da/4-Table1-1.png)
It was concluded from the results of limited structural studies that there were multiple peptide differences upon comparison of three non-α polypeptide chains in white-tailed deer. A variety of aberrant erythrocyte forms have been related to seven adult and two fetal hemoglobins in white-tailed deer. While sickling of the erythrocyte was not associated with a single hemoglobin type, it was precluded by hemoglobin V or VII, even when in combination with other hemoglobin types normally associated with sickling. The subunit basis of the hemoglobin polymorphism was presented. Two kinds of α subunits, six kinds of β subunits and one γ subunit were related to the whole hemoglobin molecule. The heterogeneity of the deer hemoglobins was based upon a variety of combinations of these numerous polypeptide chains. It was concluded from the results of limited structural studies that there were multiple peptide differences upon comparison of three non-α polypeptide chains.
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Alteration of the α1β2/α2β1 subunit interface contributes to the increased hemoglobin-oxygen affinity of high-altitude deer mice
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Alteration of the α1β2/α2β1 subunit interface contributes to the increased hemoglobin-oxygen affinity of high-altitude deer mice