Adams J G, Morrison W T, Barlow R L, Steinberg M H
V.A. Medical Center, Jackson, MS.
Hemoglobin. 1987;11(5):435-52. doi: 10.3109/03630268708998004.
Hb Mississippi was discovered in a 6-year-old Chinese girl with chronic anemia and thalassemia intermedia. Family studies revealed that she had inherited the Hb Mississippi from her father as well as inheriting a gene for beta+-thalassemia from her mother. Electrophoretic analyses of the hemolysate of the father of the father and the proband on polyacrylamide gels at pH 8.6 showed that the abnormal hemoglobin had three distinct mobilities. A similar pattern was also observed by isoelectricfocusing. In addition, multiple abnormal peaks were observed by high performance liquid chromatographic hemoglobin separations as well as high performance liquid chromatographic globin chain separation. Structural analysis of the abnormal hemoglobin demonstrated a single abnormality; the substitution of serine to cysteine at position 44 (CD3) of the beta-globin chain. Since CD3 is on the surface of the beta-globin chain, it was thought that polymerization of the abnormal hemoglobin by disulfide linkages might have been responsible for the anomalous behavior on electrophoresis and high performance liquid chromatography. Gel filtration chromatography on G-200 Sephadex confirmed this supposition and demonstrated that the abnormal globin chain polymerized with itself as well as with other globin chains.
血红蛋白密西西比型是在一名患有慢性贫血和中间型地中海贫血的6岁中国女孩身上发现的。家族研究表明，她从父亲那里遗传了血红蛋白密西西比型，同时从母亲那里遗传了一个β+地中海贫血基因。在pH 8.6条件下，对先证者及其父亲的溶血产物在聚丙烯酰胺凝胶上进行电泳分析，结果显示异常血红蛋白有三种不同的迁移率。等电聚焦也观察到了类似的模式。此外，通过高效液相色谱血红蛋白分离以及高效液相色谱珠蛋白链分离，观察到了多个异常峰。对异常血红蛋白的结构分析表明存在单一异常；β-珠蛋白链第44位（CD3）的丝氨酸被半胱氨酸取代。由于CD3位于β-珠蛋白链表面，人们认为异常血红蛋白通过二硫键聚合可能是其在电泳和高效液相色谱中出现异常行为的原因。在葡聚糖凝胶G - 200上进行的凝胶过滤色谱证实了这一推测，并表明异常珠蛋白链自身以及与其他珠蛋白链发生了聚合。
