Brown W J, Niazi G A, Jayalakshmi M, Abraham E C, Huisman T H
Biochim Biophys Acta. 1976 Jul 19;439(1):70-6. doi: 10.1016/0005-2795(76)90162-8.
A new hemoglobin variant, termed hemoglobin Athens-Georgia, has been found in a 23-year-old Caucasian student and three members of her family. The electrophoretic mobility of this variant at pH 9.0 is slightly less than that of hemoglobin-A. Arginyl residue in position 40 of the beta chain, corresponding to position 6 of the C helix, has been replaced by a lysyl residue. This amino acid substitution is at the alpha1-beta2 contact and slightly affects the oxygen binding properties of the hemoglobin molecule. Hemoglobin Athens-Georgia has an increased affinity for oxygen, a normal heme-heme interaction and a normal Bohr effect. Hematological abnormalities are not associated with this variant.
在一名23岁的白种人学生及其三名家庭成员中发现了一种新的血红蛋白变体，称为血红蛋白雅典-佐治亚。该变体在pH 9.0时的电泳迁移率略低于血红蛋白A。β链第40位的精氨酸残基（对应于C螺旋的第6位）被赖氨酸残基取代。这种氨基酸取代位于α1-β2接触点，对血红蛋白分子的氧结合特性有轻微影响。血红蛋白雅典-佐治亚对氧的亲和力增加，血红素-血红素相互作用正常，玻尔效应正常。该变体与血液学异常无关。
