scholarly journals Analysis of the specific radioactivity of valine isolated from aminoacyl-transfer ribonucleic acid of rat liver

1974 ◽  
Vol 140 (3) ◽  
pp. 545-548 ◽  
Author(s):  
C S Wallyn ◽  
A Vidrich ◽  
J Airhart ◽  
E A Khairallah
1975 ◽  
Vol 147 (3) ◽  
pp. 473-477 ◽  
Author(s):  
M Nwagwu

A procedure for preparing polyribosome aminoacyl-tRNA free from contamination by supernatant aminoacyl-tRNA and free amino acids is described. Important features of the procedure are the use of acidic buffers to help protect the amino acid-tRNA linkage and the inclusion of sodium dodecyl sulphate, to inhibit ribonuclease activity. The specific radioactivity of polyribosome aminoacyl-tRNA is high within 30s and reaches a maximum in 2 1/2 min, well ahead of polyribosome peptides which, as described by Herrmann et al. (1971), attain maximum specific radioactivity in about 10 min.


1972 ◽  
Vol 126 (4) ◽  
pp. 923-931 ◽  
Author(s):  
J. Hradec

1. Transferase I of rat liver binds aminoacyl-tRNA to form a relatively stable complex, which is retained on cellulose nitrate filters. This reaction proceeds at both 0°C and 37°C and is inhibited by GTP. The resulting product is stabilized by GTP and Mg2+. 2. Only very low quantities of deacylated tRNA are bound by transferase I. 3. Methods are described for the preparative isolation of the transferase I–aminoacyl-tRNA complex from incubation mixtures by using ion-exchange procedures. 4. The transferase I–aminoacyl-tRNA complex becomes readily bound to ribosomes. The presence of Mg2+ is essential for the binding. GTP stimulates this reaction but is not absolutely required. 5. It is concluded that the formation of the transferase I–aminoacyl-tRNA complex may be the primary reaction in the binding of aminoacyl-tRNA to mammalian ribosomes and that, unlike in bacterial systems, GTP is not absolutely required for this step.


1972 ◽  
Vol 126 (5) ◽  
pp. 1225-1229 ◽  
Author(s):  
J. Hradec

1. Transferase I from rat liver extracted with iso-octane binds significantly less aminoacyl-tRNA than the non-extracted enzyme. The original activity can be fully restored by the addition of cholesteryl 14-methylhexadecanoate. The binding capacity for GTP is not affected by the extraction. 2. In the presence of extracted transferase I the binding of aminoacyl-tRNA to ribosomes is decreased to 11–26% and the simultaneous binding of GTP to 32–43%. Cholesteryl 14-methylhexadecanoate induces a full reactivation of the extracted enzyme in both respects. 3. Extracted complexes A (aminoacyl-tRNA–GTP–transferase I) become bound to ribosomes to the same extent as the corresponding non-extracted preparations. 4. It is concluded that cholesteryl 14-methylhexadecanoate interacts with the binding site of transferase I for aminoacyl-tRNA and secondarily with that for GTP. It does not affect the binding site for ribosomes.


1981 ◽  
Vol 118 (1) ◽  
pp. 155-161 ◽  
Author(s):  
Allen M. Samarel ◽  
Edward A. Ogunro ◽  
Alan G. Ferguson ◽  
Michael Lesch

1963 ◽  
Vol 238 (4) ◽  
pp. 1479-1484 ◽  
Author(s):  
June M. Fessenden ◽  
Kivie Moldave

Sign in / Sign up

Export Citation Format

Share Document