Purification and properties of ribonucleic acid polymerase from rat liver mitochondria

Biochemistry ◽  
1973 ◽  
Vol 12 (25) ◽  
pp. 5096-5101 ◽  
Author(s):  
Himansu Mukerjee ◽  
Anna Goldfeder
Keyword(s):  
Rat Liver ◽  
Ribonucleic Acid ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Purification And Properties

Purification and Properties of Deoxyadenosine Kinase from Rat Liver Mitochondria

1984 ◽  
Vol 31 (1) ◽  
pp. 33-38
Author(s):  
Janusz Greger ◽  
K. Fabianowska-Majewska ◽  
Bogdana Gorzkiewicz
Keyword(s):  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Purification And Properties

scholarly journals Partial purification and properties of rat liver mitochondrial polynucleotide phosphorylase

1972 ◽  
Vol 130 (2) ◽  
pp. 343-353 ◽  
Author(s):  
Y. P. See ◽  
P. S. Fitt
Keyword(s):  
Rat Liver ◽  
Kinase Activity ◽  
Liver Mitochondria ◽  
Partial Purification ◽  
Rat Liver Mitochondria ◽  
Polynucleotide Phosphorylase ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Purification And Properties ◽  
Exchange Activity

1. Polynucleotide phosphorylase was partially purified from the inner membrane of rat liver mitochondria. 2. The partially purified particulate enzyme catalyses phosphorolysis of poly(A), poly(C), poly(U) and RNA to nucleoside diphosphates. 3. It is devoid of nucleoside diphosphate-polymerization activity. 4. Variable amounts of ADP/Pi-exchange activity are associated with the polynucleotide phosphorylase and are probably due to a different enzyme. 5. ADP is the preferred substrate for exchange, and little or no reaction occurs with other nucleoside diphosphates, but ATP/Pi-exchange takes place at one-third the rate observed with ADP. 6. The partially purified enzyme is free from the phosphatases found in the crude mitochondrial inner membrane, but is associated with an endonuclease activity and some adenylate kinase activity; no cytidylate kinase activity analogous to the latter was detectable.

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