Wajcman H, Delaunay J, Francina A, Rosa J, Galacteros F
INSERM U299, Hôpital de Bicêtre, Le Kremlin Bicêtre, France.
Biochim Biophys Acta. 1989 Sep 14;998(1):25-31. doi: 10.1016/0167-4838(89)90114-3.
The most striking fact in Hb Nouakchott [alpha 114(GH2)Pro----Leu] is the highly increased hydrophobicity of the abnormal chain. In comparison to other variants carrying the same amino-acid substitution, but at another position, the involvement of the environmental domains in the expression of the hydrophobicity is shown. Even though the substitution concerned a proline residue, it was without consequences on the oxygen binding and the stability of the molecule.
血红蛋白努瓦克肖特[α114(GH2)脯氨酸→亮氨酸]最显著的事实是异常链的疏水性大幅增加。与其他在不同位置携带相同氨基酸替代的变体相比,表明了环境结构域在疏水性表达中的作用。尽管该替代涉及一个脯氨酸残基,但它对氧结合和分子稳定性没有影响。