Harano T, Harano K, Shibata S, Ueda S, Imai K, Tsuneshige A, Yamada H, Seki M, Fukui H
FEBS Lett. 1983 Mar 21;153(2):332-4. doi: 10.1016/0014-5793(83)80636-x.
A new abnormal hemoglobin, Hb Kariya [alpha 40 (C5) Lys leads to Glu], with an amino acid substitution at the alpha 1 beta 2 contact was discovered in a young Japanese man. This variant migrated to the anode faster than Hb A, being nearly the same as Hb I in electrophoretic mobility. It amounted to about 6% of the total hemoglobin of the hemolysate. This hemoglobin showed an increased oxygen affinity, decreased heme-heme interaction and a lowered 2,3-DPG effect.
在一名年轻日本男性中发现了一种新的异常血红蛋白，即Hb Kariya [α40 (C5) 赖氨酸突变为谷氨酸]，其在α1β2接触位点存在氨基酸替换。该变体在电泳时向阳极迁移的速度比Hb A快，电泳迁移率与Hb I几乎相同。它占溶血产物中总血红蛋白的约6%。这种血红蛋白表现出氧亲和力增加、血红素 - 血红素相互作用降低以及2,3 - 二磷酸甘油酸（2,3-DPG）效应减弱。
