Esterase isozymes of Apis mellifera: substrate and inhibition characteristics, developmental ontogeny, and electrophoretic variability.
Starch gel electrophoresis utilizing different types of substrates and inhibitors made it possible to detect several esterases in crude extracts of Apis mellifera. Our results suggest that there are six Apis mellifera esterase isozymes (esterases 1-6) that differ not only in electrophoretic mobility but also in substrate specificity and inhibition properties. Some of the esterase isozymes are controlled by more than one allele. The frequency of these genetic variants was analyzed in four populations of Apis mellifera from several localities. Esterases 1, 2, and 4 do not exhibit developmental changes, but the electrophoretic profile of esterases 3, 4, and 6 varies during ontogenetic development.
D000483:Alleles; D000818:Animals; D001516:Bees / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D004592:Electrophoresis, Starch Gel / Q000379:methods; D004950:Esterases / Q000235:genetics* / Q000378:metabolism; D014644:Genetic Variation; D005838:Genotype; D007527:Isoenzymes / Q000235:genetics* / Q000378:metabolism; D007700:Kinetics; D007814:Larva / Q000201:enzymology; D013045:Species Specificity; D013379:Substrate Specificity
D007527:Isoenzymes; D004950:Esterases