In vitro localization of the protein synthesis defect associated with experimental phenylketonuria.
We have used a cell-free system derived from hamster brain to investigate protein synthesis during experimental phenylketonuria. In such a system the elongation inhibitor emetine impeded translation in extracts derived from both treated and control animals. On the other hand the initiation inhibitor aurintricarboxylic acid showed no effects on protein synthesis activity of treated hamsters, although it was severely inhibiting in controls. This suggests that initiation is the altered step in brain protein synthesis failure consecutive to phenylketonuria.
Elsliger
M A
MA
Département de chimie et biochimie, Université de Moncton, Canada.
Thériault
G R
GR
Gauthier
D
D
D000818:Animals; D001312:Aurintricarboxylic Acid / Q000494:pharmacology*; D006224:Cricetinae; D003509:Cyclohexanecarboxylic Acids / Q000494:pharmacology*; D004195:Disease Models, Animal; D004640:Emetine / Q000494:pharmacology; D066298:In Vitro Techniques; D010442:Peptide Chain Initiation, Translational / Q000187:drug effects*; D010661:Phenylketonurias / Q000378:metabolism*; D014176:Protein Biosynthesis / Q000187:drug effects*
D003509:Cyclohexanecarboxylic Acids; D001312:Aurintricarboxylic Acid; D004640:Emetine