Hemoglobin Columbia Missouri or alpha 2[88 (F9) Ala----Val]beta 2: a new high-oxygen-affinity hemoglobin that causes erythrocytosis.
Hemoglobin Columbia Missouri or alpha 2[88 (F9) Ala----Val]beta 2: a new high-oxygen-affinity hemoglobin that causes erythrocytosis.
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哥伦比亚密苏里血红蛋白或 α 2[88 (F9) Ala----Val]beta 2：一种新的高氧亲和力血红蛋白，可导致红细胞增多。
DOI：
10.1016/s0025-6196(12)61169-0
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发表时间：
1991
影响因子：
8.9
通讯作者：
Proud,V
中科院分区：
文献类型：
--
作者：
Perry,MC;Head,C;Fairbanks,VF;Jones,RT;Taylor,H;Proud,V
在一名正在接受红细胞增多症评估的22岁白色男性中检测到一种以前未描述的血红蛋白变体，即血红蛋白哥伦比亚密苏里州，α88（F9）Ala→瓦尔。这种新的血红蛋白变体不能通过常规介质中的电泳、等电聚焦或在8 M尿素中纯化的珠蛋白链的电泳与血红蛋白A分离。它表现出高的氧亲和力，患者全血的P50（50%饱和度下的氧张力）为19.3 mmHg。血红蛋白哥伦比亚密苏里州的取代是α链F螺旋末端附近的内部残基。冈崎血红蛋白在β链的F9（β93）处有一个半胱氨酰残基被一个β-酰基残基取代。与冈崎血红蛋白相比，哥伦比亚密苏里州血红蛋白中的取代对氧亲和力的影响更显著。因此，血红蛋白哥伦比亚密苏里州与红细胞增多症相关，而血红蛋白冈崎不相关。
A previously undescribed hemoglobin variant, hemoglobin Columbia Missouri, α88 (F9) Ala→Val, was detected in a 22-year-old white man who was undergoing assessment for erythrocytosis. This new hemoglobin variant does not separate from hemoglobin A by electrophoresis in conventional media, by isoelectric focusing, or by electrophoresis of purified globin chains in 8 M urea. It exhibits a high oxygen affinity, with a P50(oxygen tension at 50% saturation) of 19.3 torr for the patient's whole blood. The substitution of hemoglobin Columbia Missouri is an internal residue near the end of the F helix of the α chain. Hemoglobin Okazaki has an arginyl residue substitution for a cysteinyl residue at F9 (β93) in the β chain. In comparison with hemoglobin Okazaki, the substitution in hemoglobin Columbia Missouri has a more pronounced effect on oxygen affinity. Consequently, hemoglobin Columbia Missouri is associated with erythrocytosis, whereas hemoglobin Okazaki is not.