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.

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Bibliographische Detailangaben
Veröffentlicht in:	Science (American Association for the Advancement of Science) 1972-11, Vol.178 (4061), p.639-640
Hauptverfasser:	Jacob, Samson T., Schindler, Daniel G., Morris, Harold P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Animal feeding behavior Animals Carcinoma, Hepatocellular - enzymology Cytosine Nucleotides - metabolism Enzyme activity Enzymes Guanosine Triphosphate - metabolism Hepatocellular carcinoma Liver Liver Neoplasms - enzymology Messenger RNA Mitochondria Mitochondria, Liver - enzymology Neoplasms, Experimental - enzymology Nucleotides Nucleotidyltransferases - metabolism Rats Ribonucleases - pharmacology RNA RNA Nucleotidyltransferases - isolation & purification Tritium Tumors Uracil Nucleotides - metabolism
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Beschreibung
Zusammenfassung:	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.
ISSN:	0036-8075 1095-9203
DOI:	10.1126/science.178.4061.639