Genetic, ontogenetic, and tissue-specific variation of aminopeptidases of Apis mellifera

Four aminopeptidases were detected in Apis mellifera by starch gel electrop horesis. These enzymes were characterized on the basis of their substrate p reference, effect of inhibitors, tissue and ontogenetic developmental distr ibution. Lap-A activity was present at all tissues and developmental stages . Lap-P was characterized by a more intense activity during the pupal stage . Lap-G activity was concentrated in the midgut and was detected in associa tion with the presence of food inside the digestive tract. Lap-D was more p roeminent in the reproductive tract of adult drones, where its activity app eared to be concentrated in the mucus. Four electrophoretic variants of Lap -D were observed, with an uncommonly high intralocus heterozygosity level. Segregational analyses demonstrated the absence of close linkage between La p-D and Est-1a, Est-2, Est-5, Est-6, Mdh-1, Hk-1 and Pgm-1 loci of Apis mel lifera.