Bijlsma R, van der Meulen-Bruijns C
Biochem Genet. 1979 Dec;17(11-12):1131-44. doi: 10.1007/BF00504350.
The electrophoretic variants of G6PD and 6PGD isolated from the Bogota Drosophila melanogaster population were characterized developmentally and biochemically. Changes in in vitro enzyme activity during development were comparable to those found for other dehydrogenases: an increase in the larval and adult stage and a decrease in the pupal stage. During the whole life cycle the "S" enzyme of both loci showed a higher activity than the "F" enzyme. MgCl2 had a stimulating effect on the activity of both enzymes whereas their heat stability was decreased. The allozymes of 6PGD had different Vmax's but were comparable with respect to Km values, pH optimum, and stability at 45 C. the allozymes of G6PD showed different Vmax's and differed in stability at 35 C, but had similar Km values and pH optima. As the difference in stability was probably due to differences in molecular structure of the allozymes, the differences in activity found at high pH and high MgCl2 concentration were most probably due to this difference in stability.
从波哥大黑腹果蝇种群中分离出的葡萄糖-6-磷酸脱氢酶（G6PD）和6-磷酸葡萄糖酸脱氢酶（6PGD）的电泳变体，在发育和生化方面进行了表征。发育过程中体外酶活性的变化与其他脱氢酶的变化相当：幼虫期和成虫期增加，蛹期减少。在整个生命周期中，两个位点的“S”酶活性均高于“F”酶。氯化镁对两种酶的活性有刺激作用，而它们的热稳定性降低。6PGD的同工酶具有不同的最大反应速度（Vmax），但在米氏常数（Km）值、最适pH值和45℃稳定性方面相当。G6PD的同工酶显示出不同的Vmax，在35℃稳定性不同，但具有相似的Km值和最适pH值。由于稳定性差异可能是由于同工酶分子结构的差异，在高pH值和高氯化镁浓度下发现的活性差异很可能是由于这种稳定性差异。
