Adachi K, Rappaport E, Eck H S, Konitzer P, Kim J, Surrey S
Children's Hospital of Philadelphia, Division of Hematology, University of Pennsylvania School of Medicine, Philadelphia 19104.
Hemoglobin. 1991;15(5):417-30. doi: 10.3109/03630269108998861.
In an effort to clarify the role of amino acid hydrophobicity at the beta 6 position in sickling we have made recombinant hemoglobin tetramers containing beta 6 Val (Hb S) and beta 6 Leu (Hb Leu). Recombinant Hb S and Hb Leu had the same electrophoretic mobility, chromatographic behavior, and absorption spectrum. The deoxy form of both tetramers polymerized in high phosphate buffer (1.8 M) and exhibited distinct delay times prior to polymerization. The kinetics of polymerization for recombinant and native Hb S were similar, while recombinant Hb Leu polymerized more readily. The solubility of deoxy Hb Leu was less than deoxy Hb S, indicating that rapid polymerization and decreased solubility of deoxyhemoglobin is accelerated with increasing hydrophobicity at the beta 6 position.
为了阐明β6位氨基酸疏水性在镰状化过程中的作用，我们制备了含有β6缬氨酸（Hb S）和β6亮氨酸（Hb Leu）的重组血红蛋白四聚体。重组Hb S和Hb Leu具有相同的电泳迁移率、色谱行为和吸收光谱。两种四聚体的脱氧形式在高磷酸盐缓冲液（1.8 M）中聚合，并在聚合前表现出明显的延迟时间。重组Hb S和天然Hb S的聚合动力学相似，而重组Hb Leu更容易聚合。脱氧Hb Leu的溶解度低于脱氧Hb S，这表明随着β6位疏水性的增加，脱氧血红蛋白的快速聚合和溶解度降低会加速。
