Antigenotoxic and Anticarcinogenic Effects of Thiols. In Vitro Inhibition of the Mutagenicity of Drug Nitrosation Products and Protection of Rat Liver ADP-Ribosyl Transferase Activity

1988 ◽  
pp. 75-86 ◽  
Author(s):  
Silvio De Flora ◽  
Carmelo F. Cesarone ◽  
Carlo Bennicelli ◽  
Anna Camoirano ◽  
Domizio Serra ◽  
...  
1977 ◽  
Vol 164 (3) ◽  
pp. 685-691 ◽  
Author(s):  
E Marra ◽  
S Doonan ◽  
C Saccone ◽  
E Quagliariello

1. A method was devised to allow determination of intramitochondrial aspartate amino-transferase activity in suspensions of intact mitochondria. 2. Addition of purified rat liver mitochondrial aspartate aminotransferase to suspensions of rat liver mitochondria caused an apparent increase in the intramitochondrial enzyme activity. No increase was observed when the mitochondria were preincubated with the purified cytoplasmic isoenzyme. 3. These results suggest that mitochondrial aspartate aminotransferase, but not the cytoplasmic isoenzyme, is able to pass from solution into the matrix of intact rat liver mitochondria in vitro. 4. This system may provide a model for studies of the little-understood processes by which cytoplasmically synthesized components are incorporated into mitochondria in vivo.


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