Moo-Penn W F, Johnson M H, McGuffey J E, Jue D L
Hemoglobin. 1984;8(6):583-93. doi: 10.3109/03630268408991743.
Hemoglobin Shelby, detected in two unrelated black families, has an electrophoretic mobility like Hb F on cellulose acetate (pH 8.4) and a mobility between Hbs S and C on citrate agar (pH 6.2). Globin chain analysis in acid and alkaline buffers revealed an abnormal chain migrating between beta A and beta S. Tests for unstable hemoglobins were positive. Hematologic data on both families indicated carriers have mild anemia. The variant showed a slightly lower affinity for oxygen with normal cooperativity and Bohr effect, and its reactions with 2,3-diphosphoglycerate and inositol hexaphosphate were similar to those of Hb A. Sequence analysis indicated the substitution of lysine for glutamine at position 131 in the beta-chain. In a previous report (1) we described a variant, Hb Deaconess, in which this residue was deleted. On reexamination of the data, we find that Hb Deaconess is identical to Hb Shelby.
在两个无亲缘关系的黑人家庭中检测到的血红蛋白谢尔比，在醋酸纤维素（pH 8.4）上的电泳迁移率与血红蛋白F相似，在柠檬酸盐琼脂（pH 6.2）上的迁移率介于血红蛋白S和C之间。在酸性和碱性缓冲液中进行的珠蛋白链分析显示，有一条异常链在βA和βS之间迁移。不稳定血红蛋白检测呈阳性。两个家庭的血液学数据表明，携带者有轻度贫血。该变体对氧的亲和力略低，具有正常的协同性和玻尔效应，其与2,3-二磷酸甘油酸和肌醇六磷酸的反应与血红蛋白A相似。序列分析表明，β链第131位的谷氨酰胺被赖氨酸取代。在之前的一份报告（1）中，我们描述了一种变体血红蛋白迪肯尼斯，该位点的这个残基在其中被删除。在重新审查数据时，我们发现血红蛋白迪肯尼斯与血红蛋白谢尔比相同。
