Asparaginase action: Inhibition of protein synthesis in rat liver mitochondria and microsomes and brain mitochondria and inhibition of glycoprotein synthesis in liver and brain mitochondria by asparaginase

Tofranil inhibits the respiratory activity of rat brain cortex slices incubated in a glucose-containing medium. It also inhibits the uptake and incorporation of glycine-1-C14at concentrations which have only a slight inhibitory effect on the respiration of slices. Tofranil also inhibits oxidative phosphorylation in both rat liver and rat brain mitochondria but at higher concentrations respiration is greatly affected. Tofranil differs quantitatively from chlorpromazine in its greater inhibitory effect on the ATP–Pi32exchange reaction and its lesser effect on the cytochrome c oxidase activity of rat liver mitochondria.

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RNA and protein synthesis by sterile rat-liver mitochondria

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis ◽

10.1016/0005-2787(67)90639-9 ◽

1967 ◽

Vol 142 (2) ◽

pp. 552-554 ◽

Cited By ~ 25

Author(s):

A.M. Kroon ◽

C. Saccone ◽

M.J. Botman

Keyword(s):

Protein Synthesis ◽

Rat Liver ◽

Liver Mitochondria ◽

Rat Liver Mitochondria ◽

Rna And Protein Synthesis

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Inhibition of protein synthesis by ricin: experiments with rat liver mitochondria and nuclei and with ribosomes from Escherichia coli

Biochemical Journal ◽

10.1042/bj1420695 ◽

1974 ◽

Vol 142 (3) ◽

pp. 695-697 ◽

Cited By ~ 20

Author(s):

Margherita Greco ◽

Lucio Montanaro ◽

Francesco Novello ◽

Cecilia Saccone ◽

Simonetta Sperti ◽

...

Keyword(s):

Escherichia Coli ◽

Protein Synthesis ◽

Rat Liver ◽

Ricinus Communis ◽

Liver Mitochondria ◽

Rat Liver Mitochondria ◽

Isolated Rat Liver ◽

Liver Nuclei ◽

Isolated Rat ◽

Liver Ribosomes

1. Ricin, a toxic protein from the seeds of Ricinus communis which inhibits poly(U)-directed polyphenylalanine synthesis by rat liver ribosomes (Montanaro et al., 1973), does not affect protein synthesis by isolated rat liver mitochondria. 2. The toxin is ineffective also on poly(U)-directed polyphenylalanine synthesis in reconstituted systems with ribosomes isolated from rat liver mitochondria or from Escherichia coli. 3. Ricin inhibits protein synthesis by isolated rat liver nuclei, but at concentrations much higher than those affecting rat liver ribosomes.

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Inhibition of mitochondrial and bacterial protein synthesis by chloramphenicol

Canadian Journal of Biochemistry ◽

10.1139/o70-077 ◽

1970 ◽

Vol 48 (4) ◽

pp. 479-485 ◽

Cited By ~ 28

Author(s):

K. B. Freeman

Keyword(s):

Protein Synthesis ◽

Mitochondrial Protein ◽

Liver Mitochondria ◽

Rat Liver Mitochondria ◽

Bacterial Protein ◽

E Coli ◽

Inhibition Of Protein Synthesis ◽

Acetyl Group ◽

Bacterial Protein Synthesis ◽

Escherichia Coli B

The structural requirements for the inhibition of protein synthesis in mitochondria and in bacterial extracts by chloramphenicol isomers and analogues are similar. D-threo-Chloramphenicol and its p-methylthio, p-methylsulfonyl, and p-sulfamoyl analogues equally inhibit protein synthesis in isolated rat-liver mitochondria and extracts of Escherichia coli B. Fifty percent inhibition is at 15 μM and 10 μM, respectively. Analogues with larger p-substituents on the phenyl ring or with an m-chloro group are less inhibitory in both systems. L-threo-Chloramphenicol and deacylated chloramphenicol do not inhibit mitochondrial protein synthesis; with a dichloroacetyl group replacing the acetyl group on chloramphenicol 50% inhibition is at 65 μM, and L-erythro-chloramphenicol is 2% as inhibitory as D-threo-chloramphenicol. The inhibition of protein synthesis in intact E. coli B is in the order: chloramphenicol > p-methylthio > p-methylsulfonyl > p-sulfamoyl, 50% inhibition being at 4 μM for chloramphenicol.

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