Post-microsomal fractions from rat brain which stimulate ribosomal amino acid incorporation

1969 ◽  
Vol 47 (2) ◽  
pp. 75-78 ◽  
Author(s):  
M. R. V. Murthy

Post-microsomal fractions from rat brain were prepared which stimulated the synthesis of protein when endogenous mRNA was available and enhanced the synthesis of polyphenylalanine in the presence of poly-U and monomeric ribosomes. The amino-acid-activating (or transfer) enzymes did not appear to be responsible for the observed effect since the reaction mixture contained sufficient amounts of these enzymes to permit an optimum rate of amino acid incorporation. The effect was not solely due to the presence of messenger or amino acid transfer RNAs since the activity of the fractions was only partly reduced by prior treatment with ribonuclease. Heating led to complete inactivation of the fractions. Results from amino-acid-incorporation experiments and from sucrose density-gradient centrifugations indicate that the effect might be produced at two levels, one at the level of formation or preservation of polyribosomal structure and the other possibly at the level of peptide bond formation.

1967 ◽  
Vol 126 (5) ◽  
pp. 923-939 ◽  
Author(s):  
Ronald S. Goor ◽  
A. M. Pappenheimer ◽  
Elizabeth Ames

Inhibition of soluble transferase II activity in cell-free systems by diphtheria toxin and NAD can be prevented or reversed in the presence of a sufficient concentration of nicotinamide. Quantitative studies on inhibition of peptide bond formation in cell-free extracts by toxin and NAD have indicated that two successive reversible reactions are involved. First, toxin and NAD interact mole for mole to form a relatively dissociable complex. This toxin-NAD complex then reacts with transferase II to form an enzymatically inactive product that is but slightly dissociated. In the presence of sufficient nicotinamide, however, the latter complex can be broken down to yield active transferase II once more. Based on the above model, an equation has been derived that accurately predicts the per cent inhibition of amino acid incorporation in cell-free systems at any given toxin and NAD level. The observed inhibition appears to be independent of the sensitivity to toxin of the cell species from which the extracts were derived, and depends only on the toxin and NAD concentrations. Although the model satisfactorily explains inhibition of peptide bond formation by toxin in cell-free systems, further assumptions are needed to explain how still lower concentrations of toxin are able to arrest protein synthesis completely in the living cell.


2021 ◽  
Author(s):  
Xiaoling Wang ◽  
Jing Li ◽  
Yujiro Hayashi

Amide linkage of glycine-amino acid was synthesized by coupling of substituted 2-(aminomethyl)malononitrile as a C-terminal glycine unit and N-terminal amine using CsOAc and O2 in aqueous solution. This is a...


Neuroreport ◽  
1994 ◽  
Vol 5 (17) ◽  
pp. 2333-2336 ◽  
Author(s):  
Anna M. Planas ◽  
Marc A. Soriano ◽  
Isidre Ferrer ◽  
Eduard Rodríguez-Farré

Science ◽  
1964 ◽  
Vol 144 (3618) ◽  
pp. 564-564
Author(s):  
C. B. Klee ◽  
L. Sokoloff

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