Mitochondrial polyriboadenylate polymerase: relative lack of activity in hepatomas.
An enzyme that polymerizes adenylate residues from adenosine triphosphate was prepared from rat liver mitochondria and compared to similar preparations from the mitochondria of three hepatomas. Enzyme activity in the hepatomas was only 1 to 2 percent of that in normal liver.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D006528:Carcinoma, Hepatocellular / Q000201:enzymology*; D003597:Cytosine Nucleotides / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D008113:Liver Neoplasms / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D009374:Neoplasms, Experimental / Q000201:enzymology; D009713:Nucleotidyltransferases / Q000378:metabolism*; D012316:RNA Nucleotidyltransferases / Q000302:isolation & purification; D051381:Rats; D012260:Ribonucleases / Q000494:pharmacology; D014316:Tritium; D014500:Uracil Nucleotides / Q000378:metabolism
D003597:Cytosine Nucleotides; D014500:Uracil Nucleotides; D014316:Tritium; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D009713:Nucleotidyltransferases; D012316:RNA Nucleotidyltransferases; D012260:Ribonucleases