6533b855fe1ef96bd12b09a5

RESEARCH PRODUCT

Immunological detection of phenylalanine hydroxylase protein in Drosophila melanogaster.

Francisco J. SilvaJuan FerréYolanda BelLuisa María BotellaRichard G. H. Cotton

subject

animal structuresPhenylalanine hydroxylaseBlotting WesternBiochemistryDrosophilidaeComplementary DNAHemolymphAnimalsMolecular Biologychemistry.chemical_classificationImmunoassaybiologyMolecular massintegumentary systemfungiPhenylalanine HydroxylaseCell Biologybiology.organism_classificationEnzymeDrosophila melanogasterchemistryBiochemistrybiology.proteinDrosophila melanogasterPupariationResearch Article

description

A monoclonal antibody raised against monkey liver phenylalanine hydroxylase (PAH) has been used to detect this protein in Drosophila melanogaster. A cross-reacting material (CRM) band of apparent molecular mass 50-52 kDa, equivalent to that deduced for the Drosophila melanogaster PAH protein based on the pah gene cDNA sequence, has been detected. This CRM was analysed throughout development and showed an equivalent pattern to that reported for PAH activity in this insect, with maxima at pupariation and at pharate adult formation. Distribution of this CRM in larval tissues, the haemolymph and the adult body is mainly restricted to the larval fat body and the adult head. Demonstration of this CRM as the PAH protein comes from the correlation between the decreased PAH enzyme activities of two mutant strains and their decreased amounts of CRM by Western blotting.

yearjournalcountryeditionlanguage
1992-10-01
https://europepmc.org/articles/PMC1133127/