血红蛋白G Waimanalo:α64Asp→Asn及其结构分析

HEMOGLOBIN G WAIMANALO:α64(E13)ASP→ASN AND ITS STRUCTURAL ANALYSIS

本文报道在湖北省鄂西土家族苗族自治州来风县血红蛋白普查中,发现一个携带有α链变异的慢泳异常血红蛋白家系,经结构分析证明:α链64位的门冬氨酸被门冬酰胺取代,为Hb G Waimanalo:α64 Asp→Asn。

During a hemoglobin survey carried out in Lai-feng, Hubei province, three members in a family carried the same electrophoretic slow moving hemoglobin variant were found. The proband was a 39-year-old male, Hanethnic group. The variant comprised 10.9% of the total hemoglobins, the HbA and HbF were 2.7% and 2.9% respectively.Globin chain electrophoresis of hemolysate showed an α-chain abnormality. The structrual analysis of the abnormal α-chain by fingerprinting and sequencing showed that the aspartic acid residue at position 64 (E13) was displaced by asparagine, and hence it was the known HbG waimanalo:64(E13) Asp→Asn.The proband had mild microcytic hypochromatic anemia, and the otherr carriers were normal. It was suggested that the cause of amemia of some heterozygoter probably be not related to Hb G waimanalo.