Town M, Athanasiou-Metaxa M, Luzzatto L
Department of Haematology, Royal Postgraduate Medical School, Hammersmith Hospital, London, United Kingdom.
Somat Cell Mol Genet. 1990 Mar;16(2):97-108. doi: 10.1007/BF01233040.
A new variant of human glucose 6-phosphate dehydrogenase (G6PD), provisionally designated G6PD Harilaou, was observed in a Greek boy affected by severe hemolytic anemia. G6PD Harilaou was associated with very severe deficiency of enzyme activity, which measured about 1% of normal in the patient's fibroblasts. By fusion of Harilaou fibroblasts with a similarly enzyme-deficient mutant CHO cell line, we have isolated a hybrid cell line that has a G6PD activity 5-10 times higher than either of the parental cells. By electrophoretic analysis we show that most of this activity is associated with a hybrid dimeric G6PD molecule consisting of one hamster and one human subunit. We suggest that this heterologous quasi-interallelic complementation is effected by a catalytically abnormal hamster subunit stabilizing a catalytically abnormal and unstable Harilaou subunit. This approach may be useful for the study of dimer formation and stability in human G6PD.
在一名患有严重溶血性贫血的希腊男孩中，观察到一种新的人类葡萄糖-6-磷酸脱氢酶（G6PD）变体，暂定为G6PD Harilaou。G6PD Harilaou与酶活性的极其严重缺乏有关，在患者的成纤维细胞中测得的酶活性约为正常水平的1%。通过将Harilaou成纤维细胞与同样缺乏该酶的突变CHO细胞系融合，我们分离出了一个杂交细胞系，其G6PD活性比任何一个亲代细胞都高5到10倍。通过电泳分析，我们表明这种活性大部分与一种由一个仓鼠亚基和一个人类亚基组成的杂交二聚体G6PD分子有关。我们认为这种异源准等位基因互补是由一个催化异常的仓鼠亚基稳定一个催化异常且不稳定的Harilaou亚基来实现的。这种方法可能对研究人类G6PD中二聚体的形成和稳定性有用。
