作者: Rustem NURTEN , Engin BERMEK
DOI: 10.1111/J.1432-1033.1980.TB05979.X
关键词:
摘要: Interactions of rat liver elongation factor 2 (EF-2) with guanine nucleotides and ribosomes were studied by equilibrium dialysis sedimentation methods. GDP (Kd= 0.5 μM) or GDP-Mg2+ (Kd=1.57 displayed a higher affinity in the formation binary complex EF-2 than GTP 2.68 μM), GTP-Mg2+ 2.77 guanosine 5′-[β,γ-methylene]triphosphate (GuoPP[CH2]P) 24.0 μM). NaIO4-oxidized (oGDP) 38 oxidized/reduced (orGDP) 27 had lower affinites to binding site on those GTP. However, oGDP, oGTP oGuoPP[CH2]P resulted stable product which could be recovered nitrocellulose filter technique sodium dodecyl sulfate/polyacrylamide gel electrophoresis. In presence new (or different conformation site) for GuoPP[CH2]P-Mg2+ 0.26 9.3 became apparent. The thus appeared favor involving triphosphates. Adenosine diphosphate ribosylated (ADP-Rib-EF-2) its turn bind ribosome high even without 0.18 μM). GuoPP[CH2]P increased some extent ADP-Rib-EF-2 ribosomal 0.05