Biochemical studies on the mechanism of action of liver poisons I. Inhibition of protein synthesis

1972 ◽  
Vol 261 (2) ◽  
pp. 487-499 ◽  
Author(s):  
G. Glaser ◽  
J. Mager
Keyword(s):  
Protein Synthesis ◽  
Mechanism Of Action ◽  
Biochemical Studies ◽  
Inhibition Of Protein Synthesis

scholarly journals Mechanism of action of a microsomal inhibitor of protein synthesis potentiated by oxidized glutathione

1973 ◽  
Vol 136 (2) ◽  
pp. 335-342 ◽  
Author(s):  
H. T. R. Rupniak ◽  
R. V. Quincey
Keyword(s):  
Protein Synthesis ◽  
Mechanism Of Action ◽  
Nucleoside Triphosphate ◽  
Oxidized Glutathione ◽  
Direct Inhibition ◽  
Nucleoside Triphosphate Diphosphohydrolase ◽  
Inhibition Of Protein Synthesis ◽  
Inhibitor Of Protein Synthesis

Extracts of microsomal fractions cause an inhibition of protein synthesis that is most pronounced in the presence of 0.1mm-GSSG and 0.01mm-GTP, and is abolished by thiol or 0.4mm-GTP (Scornik et al., 1967). Fractionation of microsomal extracts showed that this inhibition of protein synthesis was caused by an enzyme, nucleoside diphosphate phosphohydrolase. Direct inhibition of protein synthesis on detergent-treated polyribosomes by 0.1mm-GSSG was observed under conditions of GTP limitation induced by omission of a GTP-regenerating system, or addition of a nucleoside triphosphate diphosphohydrolase. Thus GSSG potentiated the inhibition of protein synthesis caused by an enzyme that promoted removal of GTP. The inhibition was abolished by adding 4mm-2-mercaptoethanol or 0.4mm-GTP. Nucleoside diphosphate phosphohydrolase was thought also to act by promoting removal of GTP, thus causing an inhibition of protein synthesis that was potentiated by GSSG.

THE EFFECT OF ACTINOBOLIN ON NUCLEIC ACID AND PROTEIN SYNTHESIS IN ESCHERICHIA COLI

1966 ◽  
Vol 12 (3) ◽  
pp. 515-520 ◽  
Author(s):  
D. E. Hunt ◽  
R. F. Pittillo ◽  
E. P. Johnson ◽  
F. C. Moncrief
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Nucleic Acid ◽  
Mechanism Of Action ◽  
Rna Synthesis ◽  
The Other ◽  
Cross Resistance ◽  
Inhibition Of Protein Synthesis

Actinobolin inhibits protein synthesis in Escherichia coli. When the antibiotic is added to a culture at the time of inoculation, RNA synthesis is also inhibited. Inhibition of RNA synthesis appears to be a consequence of inhibition of protein synthesis. Cross-resistance experiments suggest that the mechanism of action of actinobolin differs from that of the other inhibitors of protein synthesis, chloramphenicol and sparsomycin. Phenylalanine prevents the action of actinobolin provided the amino acid and antibiotic are added simultaneously; this effect is not observed if the phenylalanine is added 1 hour after the addition of the antibiotic. Evidence is presented that the mechanism by which phenylalanine prevents inhibition by actinobolin differs from that which has been suggested for azaserine and p-fluorophenylalanine.

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