Replacements of amino-acids in proteins and ribonucleic acid coding

1962 ◽  
Vol 27 (11) ◽  
pp. 2686-2691 ◽  
Author(s):  
I. Rychlík ◽  
F. Šorm
Keyword(s):  
1962 ◽  
Vol 48 (6) ◽  
pp. 1086-1092 ◽  
Author(s):  
F. Chapeville ◽  
F. Lipmann ◽  
G. v. Ehrenstein ◽  
B. Weisblum ◽  
W. J. Ray ◽  
...  
Keyword(s):  

1962 ◽  
Vol 40 (1) ◽  
pp. 653-666 ◽  
Author(s):  
Murray J. Fraser

A sensitive method for the measurement of amino acyl RNA synthetase activities (amino acid activating enzymes) is described. The method is based on measurements of the rates of labelling of soluble ribonucleic acid with14C-amino acids. Determinations of α-glutamyl-RNA, glutaminyl-RNA, and glycyl-RNA synthetase activities in the "pH 5 enzymes" fractions from rat liver and mouse Ehrlich ascites carcinoma cells have been made.


1969 ◽  
Vol 114 (2) ◽  
pp. 429-435 ◽  
Author(s):  
David J. Pillinger ◽  
John Hay ◽  
Ernest Borek

1. The ability of chemically hypermethylated Escherichia coli B transfer RNA to accept 19 amino acids was studied and the results were compared with those obtained with a control sample of E. coli B transfer RNA incubated under similar conditions in the absence of methylating agent. 2. There is a marked decrease in the ability of the modified transfer RNA to accept amino acids in almost all instances. 3. The acceptance of cysteine appears to be unique in that it is enhanced in the hypermethylated transfer RNA. 4. More detailed studies on the kinetics of acceptance for six amino acids is presented, emphasizing the variation in response of the individual amino acids. 5. Increasing hypermethylation causes a progressive decrease in the amino acid acceptance. 6. The results are discussed in terms of methylation at functional sites within the transfer RNA and possible conformational alterations to the structure of the macromolecule.


1962 ◽  
Vol 40 (5) ◽  
pp. 653-666 ◽  
Author(s):  
Murray J. Fraser

A sensitive method for the measurement of amino acyl RNA synthetase activities (amino acid activating enzymes) is described. The method is based on measurements of the rates of labelling of soluble ribonucleic acid with14C-amino acids. Determinations of α-glutamyl-RNA, glutaminyl-RNA, and glycyl-RNA synthetase activities in the "pH 5 enzymes" fractions from rat liver and mouse Ehrlich ascites carcinoma cells have been made.


1970 ◽  
Vol 117 (5) ◽  
pp. 853-859 ◽  
Author(s):  
T. C. Hall ◽  
K. L. Tao

1. A procedure for measuring rates of aminoacyl-tRNA synthesis in vitro and in intact leaves is presented. 2. Leaf discs showed rates close to those of intact leaves. 3. Cell-free preparations showed similar rates when assayed by pyrophosphate exchange, but actual aminoacyl-tRNA formation rates appeared to be much lower. Evidence is presented that dilution of supplied labelled amino acids was a major factor causing the low apparent rates. 4. Attempts to strip endogenous amino acids from plant tRNA resulted in low acceptor capability of the tRNA.


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