Inhibition of protein synthesis by glucose 6-phosphate and fructose 1,6-diphosphate in lysed rabbit reticulocytes and the reversal of inhibition by NAD +

1978 ◽  
Vol 82 (3) ◽  
pp. 921-928 ◽  
Author(s):  
Joseph M. Wu ◽  
Chi P. Cheung ◽  
Robert J. Suhadolnik
Keyword(s):  
Protein Synthesis ◽  
Inhibition Of Protein Synthesis ◽  
Rabbit Reticulocytes

scholarly journals Inhibition of protein synthesis by a toxic lectin from Viscum album L. (mistletoe)

1980 ◽  
Vol 190 (3) ◽  
pp. 843-845 ◽  
Author(s):  
F Stirpe ◽  
R F Legg ◽  
L J Onyon ◽  
P Ziska ◽  
H Franz
Keyword(s):  
Protein Synthesis ◽  
Viscum Album ◽  
Lag Time ◽  
Cells In Culture ◽  
Inhibition Of Protein Synthesis ◽  
Gross Lesions ◽  
Rabbit Reticulocytes

1. The haemagglutinating and toxic lectin from Viscum album L. (mistletoe) inhibits protein synthesis in a lysate of rabbit reticulocytes, with an ID50 (concentration giving 50% inhibition) of 2.6 microgram/ml. This effect is enhanced (ID50 0.21 microgram/ml) if the lectin is reduced with 2-mercaptoethanol. 2. The lectin inhibits protein synthesis also in BL8L cells in culture. Inhibition occurs after a lag time of 3 h. The ID50 is 7 ng/ml, and increases after reduction of the lectin. 3. This and the gross lesions observed in rats poisoned with V. album lectin indicate this is a toxin very similar to ricin.

Phosphorylation and the control of protein synthesis

1983 ◽  
Vol 302 (1108) ◽  
pp. 127-134 ◽  
Keyword(s):  
Protein Synthesis ◽  
Protein Kinases ◽  
Molecular Mechanism ◽  
The Other ◽  
Initiation Factor ◽  
Reversible Phosphorylation ◽  
Double Stranded Rna ◽  
Inhibition Of Protein Synthesis ◽  
The One ◽  
Rabbit Reticulocytes

This paper reviews the evidence that protein synthesis in rabbit reticulocytes is regulated by the reversible phosphorylation of the initiation factor eIF-2 by protein kinases under the control of the cytoplasmic haemin concentration on the one hand, and double-stranded RNA on the other. A molecular mechanism is proposed to account for the observation that inhibition of protein synthesis occurs when considerably less than half the eIF-2 present has been phosphorylated. The question of whether phosphorylation regulates protein synthesis in other types of cell is discussed.

scholarly journals Modeccin, the toxin of Adenia digitata. Purification, toxicity and inhibition of protein synthesis in vitro

1978 ◽  
Vol 174 (2) ◽  
pp. 491-496 ◽  
Author(s):  
A Gasperi-Campani ◽  
L Barbieri ◽  
E Lorenzoni ◽  
L Montanaro ◽  
S Sperti ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Affinity Chromatography ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Cells ◽  
Inhibition Of Protein Synthesis ◽  
Sepharose 4B ◽  
Rabbit Reticulocytes ◽  
In Cells

1. Modeccin, the toxin of Adenia digitata (Modecca digitata), was purified from the roots of this plant by affinity chromatography on Sepharose 4B. 2. This toxin is a protein with mol.wt. 57000, which on treatment with 2-mercaptoethanol can be dissociated into two subunits of mol.wts. 25000 and 32000. 3. Modeccin inhibits protein synthesis in vitro in a lysate of rabbit reticulocytes and in Ehrlich ascites cells; the effect on cells is decreased in the presence of lactose. 4. Dissociation of modeccin into subunits decreases the toxicity to animals and the inhibition of protein synthesis in cells, but enhances the inhibition of protein synthesis in the lysate system.

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