scholarly journals Growth hormone and the binding of aminoacyl-transfer-ribonucleic acid to liver ribosomes

1969 ◽  
Vol 114 (4) ◽  
pp. 63P-64P ◽  
Author(s):  
C C Liew ◽  
A Korner
Keyword(s):  
Growth Hormone ◽  
Ribonucleic Acid ◽  
Aminoacyl Transfer ◽  
Liver Ribosomes

scholarly journals Intermediate reactions in the binding of aminoacyl-transfer ribonucleic acid to rat liver ribosomes. Formation and properties of an aminoacyl-transfer ribonucleic acid–transferase I complex

1972 ◽  
Vol 126 (4) ◽  
pp. 923-931 ◽  
Author(s):  
J. Hradec
Keyword(s):  
Ion Exchange ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Cellulose Nitrate ◽  
Stable Complex ◽  
Primary Reaction ◽  
Preparative Isolation ◽  
Reaction Proceeds ◽  
Aminoacyl Transfer ◽  
Liver Ribosomes

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.

scholarly journals Intermediate reactions in the binding of aminoacyl-transfer ribonucleic acid to rat liver ribosomes. The interaction of cholesteryl 14-methylhexadecanoate

1972 ◽  
Vol 126 (5) ◽  
pp. 1225-1229 ◽  
Author(s):  
J. Hradec
Keyword(s):  
Binding Site ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Binding Capacity ◽  
Original Activity ◽  
Aminoacyl Transfer ◽  
Liver Ribosomes

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.

scholarly journals Studies on Aminoacyl Transfer from Soluble Ribonucleic Acid to Ribosomes

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

5S Ribonucleic acid-protein complex extracted from rat liver ribosomes by formamide

Biochemistry ◽  
1972 ◽  
Vol 11 (12) ◽  
pp. 2323-2326 ◽  
Author(s):  
Mary L. Petermann ◽  
Mary G. Hamilton ◽  
Amalia Pavlovec
Keyword(s):  
Rat Liver ◽  
Protein Complex ◽  
Ribonucleic Acid ◽  
Acid Protein ◽  
Liver Ribosomes
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