No abstract

No abstract

Experiments have been performed to show that PGM polymorphism for the two common electrophoretic allozymes, PGM A and PGM B , in Drosophila melanogaster has adaptive value. Firstly, the allele frequencies converge to the same equilibrium value in six experimental populations. Secondly, density-dependent selection operates. Thirdly, the relative fitness of the three genotypes varies in modified culture media. PGM polymorphism is maintained by frequency-dependent selection and heterotic selection: the first mechanism operates to reach equilibrium frequency, the second cooperates to maintain it. The experiments performed with modified culture media favour the view that the two allozymes have different affinities for two components which are present in the nutritional environment. These components may be either substrates or other factors involved in the reaction catalyzed by PGM.

No abstract

Phosphoglucomutase (PGM) of adult stage in Drosophilia melanogaster has been characterized by gel filtration, ion-exchange chromatography, and isoelectric focusing. The two common electrophoretic variants, PGMA and PGMB, differ with respect to their kinetic and stability parameters. PGMA is more thermostable than PGMB but shows the same pH optimum, equal dependence on Mg2+, and identical molecular weight. There is no significant kinetic difference between the two allozymes at the optimum pH values, but at pH 6.0 the Km value for glucose-1,6-diphosphate of PGMB is significantly higher than that of PGMA. This difference might explain the observed selective advantage of the PgmA allele in population studies.