Stimulation by Rat Liver Ribonucleic Acid of Incorporation of Amino-acid into Rat Liver Ribosomes

Nature ◽  
1963 ◽  
Vol 199 (4892) ◽  
pp. 489-490 ◽  
Author(s):  
A. KORNER ◽  
A. J. MUNRO
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Liver Ribosomes

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

A SENSITIVE METHOD FOR MEASUREMENT OF AMINO ACYL RIBONUCLEIC ACID SYNTHETASE ACTIVITIES

1962 ◽  
Vol 40 (1) ◽  
pp. 653-666 ◽  
Author(s):  
Murray J. Fraser
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Ehrlich Ascites ◽  
Sensitive Method

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.

A SENSITIVE METHOD FOR MEASUREMENT OF AMINO ACYL RIBONUCLEIC ACID SYNTHETASE ACTIVITIES

1962 ◽  
Vol 40 (5) ◽  
pp. 653-666 ◽  
Author(s):  
Murray J. Fraser
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Ehrlich Ascites ◽  
Sensitive Method

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.

scholarly journals The effect of ribonuclease on rat-liver ribosomes

1968 ◽  
Vol 106 (1) ◽  
pp. 263-266 ◽  
Author(s):  
R. Brentani ◽  
M. Brentani ◽  
I. Raw ◽  
J. L. M. Cunha ◽  
N. Wrotschincky
Keyword(s):  
Amino Acid ◽  
Protein Content ◽  
Rat Liver ◽  
Sedimentation Coefficient ◽  
Analytical Ultracentrifuge ◽  
Amino Acid Incorporation ◽  
Protein Ratio ◽  
Acid Incorporation ◽  
Liver Ribosomes

1. Rat-liver ribosomes lose about 50% of their amino acid-incorporating activity when preincubated with ribonuclease. 2. This preincubation results also in loss of about 50% of the original protein content and 75% of the RNA. 3. Ribosomes sedimented by ultracentrifugation, after preincubation with ribonuclease, show negligible contamination by crystalline enzyme. 4. Washing of ribosomes treated with ribonuclease releases further protein, restoring the original RNA/protein ratio. 5. The washed particle is again capable of promoting amino acid incorporation. 6. Examination of ribosomes treated with ribonuclease in the analytical ultracentrifuge reveals destruction of ribosomes, disappearance of dimers and a decrease in the sedimentation coefficient of monomers. 7. Washed ribosomes consist of even smaller particles with a sedimentation coefficient 60s.

Phenylalanyl transfer ribonucleic acid synthetase activity associated with rat liver ribosomes and microsomes

Biochemistry ◽  
1973 ◽  
Vol 12 (20) ◽  
pp. 3859-3865 ◽  
Author(s):  
Joan S. Tscherne ◽  
Bernard Weinstein ◽  
Karl W. Lanks ◽  
Naola B. Gersten ◽  
Charles R. Cantor
Keyword(s):  
Rat Liver ◽  
Ribonucleic Acid ◽  
Synthetase Activity ◽  
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 Synthesis of cyclohexylpuromycin and its reaction with N-acetylphenylalanyl-transfer ribonucleic acid on rat liver ribosomes

1975 ◽  
Vol 145 (2) ◽  
pp. 169-176 ◽  
Author(s):  
M Ariatti ◽  
A O Hawtrey
Keyword(s):  
Benzene Ring ◽  
Aromatic Ring ◽  
Rat Liver ◽  
Ribonucleic Acid ◽  
Ring System ◽  
Cyclohexane Ring ◽  
Liver Ribosomes

1. Cyclohexylpuromycin, an anlogue of puromycin in which a cyclohexane ring replaces the aromatic benzene ring of the L-phenylalanyl moeity of the nucleoside., has been synthesized and examined for its ability to release N-acetylphenylalanine from tRNA attached to rat liver ribosomes. 2.dl-Cyclohexylpuromycin was active in reacting with N-[3H]acetylphenylalanyl-tRNA on rat liver ribosomes to form N-E13H]lacetylphenylalanycyclohexypuromycin. 3. The reaction product N-acetylphenylalanylcyclohexylpuromycin and the corresponding analogue N-acetylphenylalanylpuromycin were chemically synthesized for evaluation of the structure of the released N-acetylphenylalanyl-containing material. 4. The results obtained suggest that the model of Raacke (1971) for purmycin reactivity needs further examination with regard to the role played by the aromatic ring system of the Lphenylalanyl moiety of the nucleoside

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