Jones R T, Koler R D, Duerst M L, Dhindsa D S
Hemoglobin. 1976;1(1):45-57. doi: 10.3109/03630267609031021.
A hemoglobin variant with the same electrophoretic mobility as hemoglobin S was found in three generations of a black family. No clinical symptoms or findings were present in subjects heterozygous for this mutant. Except for target forms of mature erythrocytes, they have no abnormal hematologic findings. Structural studies demonstrated a previously undescribed substitution, beta51 Pro replaced by Arg, in the abnormal fraction which accounts for about one-third of the total hemoglobin. This fraction is more unstable in vitro at 65 degrees than normal A hemoglobin. Both whole blood and purified abnormal hemoglobin have increased oxygen affinity and a slightly decreased Bohr effect.
在一个黑人家庭的三代人中发现了一种与血红蛋白S具有相同电泳迁移率的血红蛋白变体。该突变杂合子个体没有临床症状或体征。除了成熟红细胞的靶形形态外，他们没有异常的血液学表现。结构研究表明，在占总血红蛋白约三分之一的异常组分中，存在一种先前未描述的替代，即β51位的脯氨酸被精氨酸取代。该组分在65摄氏度下体外比正常A血红蛋白更不稳定。全血和纯化的异常血红蛋白都具有增加的氧亲和力和略微降低的玻尔效应。
