Abstract
The method allows the determination of the activity level of enzymes in a single fly and assessing the genetic composition of the given individual at these enzyme loci. Three isofemale lines were constructed which were monomorphic at several enzyme loci. Samples were prepared in two different ways: (i) individual samples--individuals were homogenised separately; (ii) collective samples--a common homogenate was prepared from several individuals. Oregon-R strain was also used to prepare a standard homogenate. The activities of alcohol dehydrogenase (ADH), alpha-glycerophosphate dehydrogenase (alpha GPDH), isocitrate dehydrogenase (IDH), and 6-phosphogluconate dehydrogenase (6PGDH), were measured in each sample on starch gel after the proteins were separated by electrophoresis. Enzyme activities were assessed by the optical density of the bands. Gel and position weights were estimated on the basis of the statistical analyses of the activities measured in the standard samples. Gel weights were then used to account for the activity differences among the gels while position weights were applied to correct for the general tendencies in the activities observed within the gels. The gel and position weighted activities of individual and collective samples were compared in the isofemale lines. The individual samples had approximately two times as much variation as the collective samples for all four enzymes. The electrophoretic method is sensitive enough to study the structure of the phenotypic variation in enzyme activity in the natural populations. The total variation among the standard samples was close to the within subline component of variation obtained for the collective samples (measurement error). This shows that the standard samples can be used to estimate the size of the measurement error.
