Miyaji T, Oba Y, Yamamoto K, Shibata S, Iuchi I, Hamilton H B
Science. 1968 Jan 12;159(3811):204-6. doi: 10.1126/science.159.3811.204.
A variant of hemoglobin A, named Hb Hijiyama, found in two generations of a Japanese family living in Hiroshima, Japan, has a higher anodal electrophoretic mobility than hemoglobin A; a gain of two negative charges per molecule is indicated. Fingerprinting and amino acid analysis showed the biochemical anomaly to be in the beta chain at residue 120, where lysine is replaced by glutamic acid. In the heterozygote carriers of the abnormal hemoglobin there is no apparent association with clinical or hematologic abnormalities.
在居住于日本广岛的一个日本家庭的两代人中发现了一种血红蛋白A的变体,名为Hb Hijiyama,它的阳极电泳迁移率比血红蛋白A高;这表明每个分子增加了两个负电荷。指纹图谱和氨基酸分析表明,生化异常发生在β链的第120位残基处,赖氨酸被谷氨酸取代。在异常血红蛋白的杂合子携带者中,未发现与临床或血液学异常有明显关联。