Harano T, Harano K, Kushida Y, Ueda S, Yoshii A, Nishinarita M
Department of Biochemistry, Kawasaki Medical School, Kurashiki, Japan.
Hemoglobin. 1991;15(4):279-90. doi: 10.3109/03630269109027880.
A 50-year-old Japanese female patient was found to have hemolytic anemia. Isoelectrofocusing of her hemolysate revealed two abnormal hemoglobin bands, one of which was very close to the Hb A2 band, and the other between the Hb A2 and Hb F bands. CM-cellulose column chromatography of the globin prepared from the abnormal hemoglobin showed that the abnormal chain eluted faster than the normal beta and delta chains; the beta X chain, however, did not separate from the normal beta chain in urea cellulose acetate electrophoresis. An instability test of the patient's hemolysate revealed the presence of an unstable component. Structural analysis of the abnormal beta chain indicated that the histidine residue at beta 92(F8) was replaced by an asparagine or aspartic acid residue. DNA amplified by polymerase chain reaction was sequenced by the dideoxy method. The nucleotide sequence of the beta 92 codon was AAC instead of CAC, suggesting that the amino acid substitution corresponded to His----Asn, which is the same as is found in Hb Redondo or beta 92(F8)His----Asn----Asp.
一名50岁的日本女性患者被诊断为溶血性贫血。对其溶血产物进行等电聚焦分析，发现两条异常血红蛋白带，其中一条非常接近Hb A2带，另一条位于Hb A2和Hb F带之间。对由异常血红蛋白制备的珠蛋白进行CM - 纤维素柱层析分析，结果显示异常链比正常的β链和δ链洗脱得更快；然而，在尿素纤维素醋酸酯电泳中，βX链并未与正常β链分离。对患者溶血产物进行的稳定性测试表明存在不稳定成分。对异常β链的结构分析表明，β92（F8）位的组氨酸残基被天冬酰胺或天冬氨酸残基取代。通过聚合酶链反应扩增的DNA采用双脱氧法进行测序。β92密码子的核苷酸序列为AAC而非CAC，这表明氨基酸替代为His→Asn，与Hb Redondo或β92（F8）His→Asn→Asp中的情况相同。
