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

Abstract

Four aminopeptidases were detected in Apis mellifera by starch gel electrophoresis. These enzymes were characterized on the basis of their substrate preference, effect of inhibitors, tissue and ontogenetic developmental distribution. 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 association with the presence of food inside the digestive tract. Lap-D was more proeminent in the reproductive tract of adult drones, where its activity appeared 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 Lap-D and Est-1a, Est-2, Est-5, Est-6, Mdh-1, Hk-1 and Pgm-1 loci of Apis mellifera.