Alcohol dehydrogenase polymorphism in Apis mellifera.
A polymorphic system of ADH isozymes is described in the honeybee Apis mellifera. Three and six different electrophoretic patterns were found, respectively, in drone and worker pupae analysis. The data indicate that the ADH isozymes are controlled by three alleles, Adh-1(1), Adh-1(2), and Adh-1(3). The frequency of the Adh-1 alleles is different in two analyzed subspecies, Apis mellifera adansonii (African bees) and Apis mellifera ligustica (Italian bees). In the African bees, the frequencies are 0.256 and 0.697 for Adh-1(1) and Adh-1(2), respectively. In the Italian bees, these values are shown to be 0.902 and 0.098, respectively. The allele Adh-1(3) was not detected in the Italian bee population. The effect of NAD on the resolution of this system was investigated, and only one region of ADH activity was obtained in drone pupae analysis when NAD was used in the gels. However, two different regions of activity were observed in the same samples, in the absence of the coenzyme. ADH activity was not detected in young larvae, but it increased to a maximum in prepupal and white-eyed pupal phases. It then declined progressively to total absence in the emerging bees.
D000429:Alcohol Oxidoreductases / Q000378:metabolism; D000483:Alleles; D000818:Animals; D001516:Bees / Q000201:enzymology*; D003433:Crosses, Genetic; D004592:Electrophoresis, Starch Gel; D005260:Female; D014644:Genetic Variation; D005838:Genotype; D006824:Hybridization, Genetic; D007527:Isoenzymes / Q000378:metabolism; D008297:Male; D011110:Polymorphism, Genetic; D013045:Species Specificity
D007527:Isoenzymes; D000429:Alcohol Oxidoreductases