A translational inhibitor activated in rabbit reticulocyte lysates under high pO2.
An inhibitor of protein synthesis was activated under high oxygen partial pressure (pO2) in hemin-supplemented and glutathione disulfide-free lysates from rabbit reticulocytes. This inhibitor shared some common features with other translational inhibitors from rabbit reticulocytes; that is, hemin-controlled repressor, glutathione disulfide-activated inhibitor and high pressure-activated inhibitor. It caused biphasic kinetics of inhibition which could be potentiated by ATP. Its activation was prevented by cAMP or glucose 6-phosphate. The high pO2-inhibitor could be partially purified from post-ribosomal supernatant containing ribosomal salt wash by precipitation between 0-50% (NH4)2SO4-saturation, Sephadex G-100, and DEAE-cellulose chromatography.
D000818:Animals; D002850:Chromatography, Gel; D000242:Cyclic AMP / Q000494:pharmacology; D005958:Glucosephosphates / Q000494:pharmacology; D005978:Glutathione / Q000494:pharmacology; D010100:Oxygen; D014176:Protein Biosynthesis / Q000187:drug effects*; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism*
D005958:Glucosephosphates; D000242:Cyclic AMP; D005978:Glutathione; D010100:Oxygen