The functional significance of amylase polymorphism in Drosophila melanogaster I. Properties of two amylase variants
The functional significance of amylase polymorphism in Drosophila melanogaster I. Properties of two amylase variants
复制标题
果蝇淀粉酶多态性的功能意义 I. 两种淀粉酶变体的特性
DOI:
10.1007/bf00120563
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发表时间:
1978
期刊:
影响因子:
1.5
通讯作者:
W. Scharloo
中科院分区:
文献类型:
--
作者:
A. Hoorn;W. Scharloo
Properties of amylase of two strains homozygous for two different amylase variants of Drosophila rnelanogaster were determined. Amylase of larvae and adults of both strains showed a pH optimum around pit 7.0. The Amy I enz)alae showed a higher temperature stability. They differed in maximal activity (for Amy 1 Vma x = 26.2 mU/9, for Amy4, 6 Vma x = 128.9 mU/ 9) and Michaelis constants (for Amy 1 K m = 0.09% starch, for Amy a,6 K m = 0.25% starch). This means that the activity difference measured at saturating substrate concentrations will not vanish or will not be reversed at lower substrate concentrations. This supports the hypothesis that this difference in amylase activity will cause a selective advantage when the two strains compete for food and starch is a limiting factor.