Miller S, Pearcy R W, Berger E
Biochem Genet. 1975 Apr;13(3-4):175-88. doi: 10.1007/BF00486013.
A biochemical comparison was made between alpha-glycerophosphate dehydrogenase allozymes from Drosophila melanogaster. Enzymes extracted from the three major genotypes were indistinguishable in terms of their pH optima and thermal stabilities. Distinctive differences were observed for three parameters; temperature dependence of specific activity, temperature dependence of K-m, and reaction rate constancy over a physiological temperature range. These results are discussed in terms of a model of balancing selection and the existence of spatial and temporal allele frequency clines in natural populations.
对黑腹果蝇的α-甘油磷酸脱氢酶同工酶进行了生化比较。从三种主要基因型中提取的酶在最适pH值和热稳定性方面没有区别。在三个参数上观察到了显著差异;比活性的温度依赖性、米氏常数(K-m)的温度依赖性以及在生理温度范围内的反应速率恒定性。根据平衡选择模型以及自然种群中空间和时间等位基因频率渐变群的存在对这些结果进行了讨论。