Yoshida A, Stamatoyannopoulos G, Motulsky A G
Science. 1967 Jan 6;155(3758):97-9. doi: 10.1126/science.155.3758.97.
Glucose-6-phosphate dehydrogenase in erythrocytes of the Negro type associated with enzyme deficiency (A(-)) was separated by chromatography on a carboxymethyl-Sephadex column from the electrophoretically indistinguishable Negro variant with normal enzyme activity (A(+)). Quantitative immunologic neutralization tests indicated that the A(-) enzyme had about the same enzymatic and serological activity as the A(+) and the normal (B(+)) enzymes. The enzyme activity of the A(-) variant in young erythrocytes was similar to that in young cells from normal individuals, although the activity of the A(-) variant in unfractionated red cells was 10 to 15 percent of normal. These data indicate that the basic defect in the variant enzyme (A(-)) is a structural mutation which causes more rapid degradation of the enzyme during erythrocyte aging.
通过羧甲基 - 葡聚糖凝胶柱色谱法，从电泳上无法区分但具有正常酶活性的黑人变体（A(+)）中分离出了与酶缺乏相关的黑人类型红细胞中的葡萄糖 - 6 - 磷酸脱氢酶（A(-)）。定量免疫中和试验表明，A(-)酶的酶活性和血清学活性与A(+)酶和正常（B(+)）酶大致相同。年轻红细胞中A(-)变体的酶活性与正常个体年轻细胞中的酶活性相似，尽管未分级红细胞中A(-)变体的活性仅为正常活性的10%至15%。这些数据表明，变体酶（A(-)）的基本缺陷是一种结构突变，它导致该酶在红细胞衰老过程中更快地降解。
