Please use this identifier to cite or link to this item: https://repositorio.inpa.gov.br/handle/1/16462
Title: Biology of Amazonian anopheline. XX. Ontogeny of esterases, leucine aminopeptidase and alpha-glycerophosphate dehydrogenase in Anopheles (Nyssorhynchus) darlingi Root, 1926 (Diptera, Culicidae).
Authors: Santos, Joselita Maria Mendes dos
Tadei, Wanderli Pedro
Contel, Eucléia Primo Betioli
Keywords: Cytosol Aminopeptidase
Esterases
Glycerol 3 Phosphate Dehydrogenase
Animals
Anopheles
Enzymology
Gene Expression
Genetics
Growth, Development And Aging
Metabolism
Animal
Anopheles
Esterases
Gene Expression
Glycerolphosphate Dehydrogenase
Leucyl Aminopeptidase
Issue Date: 1996
metadata.dc.publisher.journal: Revista Brasileira de Biologia
metadata.dc.relation.ispartof: Volume 56, Número 3, Pags. 591-598
Abstract: The esterases, leucine aminopeptidase and alpha-glycerophosphate dehydrogenase revealed modifications in gene expressions during the development of Anopheles darlingi. The esterases showed five activity bands, 1 and 2 being more deeply stained during the larval stages than in pupae or adults, esterases 3 and 4 more deeply stained in pupae and adults whereas esterase 5 was present throughout development. Leucine aminopeptidase showed five activity bands: LAP2 and LAP5 were characteristic of larvae, LAP3 was specific for pupae and adults, LAP4 was detected only in pupae, and LAP1 and LAP6 were detected in all stages. alpha-Glycerophosphate dehydrogenase presented one activity band on starch gel whose intensity increased with development. Two activity bands were detected on polyacrylamide gel (alpha-GPDH1 and alpha-GPDH2) in 4th-instar larvae (old pigmented larvae) and this activity increased with development.
Appears in Collections:Artigos

Files in This Item:
There are no files associated with this item.


This item is licensed under a Creative Commons License Creative Commons