Studies on soluble ribonucleic acid of rabbit liver. Action of polynucleotide phosphorylase

1960 ◽  
Vol 38 ◽  
pp. 568-570 ◽  
Author(s):  
Maxine F. Singer ◽  
S. Luborsky ◽  
R.A. Morrison ◽  
G.L. Cantoni
1976 ◽  
Vol 98 (16) ◽  
pp. 5044-5046 ◽  
Author(s):  
H. Kasai ◽  
K. Nakanishi ◽  
R. D. Macfarlane ◽  
D. F. Torgerson ◽  
Z. Ohashi ◽  
...  

The enzyme responsible for the breakdown of the rapidly labelled ribonucleic acid ( RNA ) in the HeLa cell nucleus has the properties of a polynucleotide phosphorylase. This enzyme acts preferentially on the rapidly labelled RNA and appears to degrade it to nucleoside-5' diphosphates. Both the rapidly labelled RNA and the enzyme which degrades it are apparently attached to the chromosome.


1975 ◽  
Vol 150 (3) ◽  
pp. 419-432 ◽  
Author(s):  
M Butler ◽  
A Darbre ◽  
H R Arnstein

1. tRNA was extracted from rabbit liver by both the phenol and diethyl pyrocarbonate methods under conditions preventing deacylation of the amino acids attached in vivo. 2. After deacylation 12 amino acids were determined by gas-liquid chromatography, by using the flame-ionization and nitrogen-sensitive thermionic detectors. 3. Comparison of the distribution of 12 amino acids attached to tRNA with those contained in total tissue protein and in the free pool showed little correlation. 4. Results for the enzymic charging assay for tRNA in vitro did not correlate satisfactorily with the analysis of amino acids attached to tRNA in vivo. Marked differences were ntoed in comparison made between our own and other published results.


1962 ◽  
Vol 237 (12) ◽  
pp. 3760-3769
Author(s):  
Kilmer S. McCully ◽  
G.L. Cantoni

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