Jones R T, Brimhall B, Huisman T H, Kleihauer E, Betke K
Science. 1966 Nov 25;154(3752):1024-7. doi: 10.1126/science.154.3752.1024.
Structural characterization of a new variant of human hemoglobin (adult), designated hemoglobin Freiburg, indicates the deletion of the valyl residue No. 23 from an otherwise normal beta-chain. The formula may be written (alpha2)beta(2)(23val-0). The abnormal hemoglobin is present with hemoglobin A in the proposita and in two of her three living children, but is not detectable in her parents. We postulate that this variant represents a triplet base deletion which most likely resulted from an unequal crossing-over between two normal betachain loci during meiosis in one of the parents of the proposita.
一种新的人类血红蛋白（成人型）变体，即弗莱堡血红蛋白的结构特征表明，在原本正常的β链中第23位缬氨酸残基缺失。其分子式可写成(α2)β(2)(23val-0)。在该先证者及其三个在世子女中的两个体内，异常血红蛋白与血红蛋白A同时存在，但在其父母体内未检测到。我们推测，这种变体代表三联体碱基缺失，很可能是由于先证者父母一方减数分裂过程中两个正常β链基因座之间发生不等交换所致。
