Hassan W, Basset P, Oudart J L, Goossens M, Rosa J
Hemoglobin. 1977;1(5):487-501. doi: 10.3109/03630267709027866.
We have previously described the structural identification of the sickle hemoglobin variant Hb C Ziguinchor (alpha2A beta2 6 Glu replaced by Val, 58 Pro replaced by Arg). This hemoglobin was found in two generations (three members) of an African family. In two family members, the clinical picture resembled that typical of a sickle cell trait, while the third member showed a more extreme clinical condition due to complication by an iron deficiency anemia. The functional properties of Hb C Zig. in red blood cells or in dilute solutions were identical to those of Hb S. The gelling behaviour of deoxy Hb C Zig. was also indistinguishable from that of Hb S. These findings suggest that, in contrast to the case of Hb C Harlem, the second substitution in position beta58 in Hb C Zig. does not interfere with the intermolecular interactions determined by the sickle substitution.
我们之前已经描述了镰状血红蛋白变体Hb C齐金乔尔（α2Aβ2 6位谷氨酸被缬氨酸取代，58位脯氨酸被精氨酸取代）的结构鉴定。这种血红蛋白在一个非洲家庭的两代人（三名成员）中被发现。在两名家庭成员中，临床表现类似于典型的镰状细胞性状，而第三名成员由于并发缺铁性贫血而表现出更严重的临床状况。Hb C Zig在红细胞或稀溶液中的功能特性与Hb S相同。脱氧Hb C Zig的凝胶化行为也与Hb S无法区分。这些发现表明，与Hb C哈莱姆的情况不同，Hb C Zig中β58位的第二个取代不会干扰由镰状取代决定的分子间相互作用。
