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PMID: 4343765 Published · ppublish English Journal Article

Mitochondrial polyriboadenylate polymerase: relative lack of activity in hepatomas.

Science (New York, N.Y.) ·Vol. 178 ·No. 4061 ·1972-11-10 ·Pages 639-40

Jacob ST, Schindler DG, Morris HP

Abstract

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.

MeSH Terms
Adenosine Triphosphate/metabolism Animals Carcinoma, Hepatocellular/enzymology Cytosine Nucleotides/metabolism Guanosine Triphosphate/metabolism Liver Neoplasms/enzymology Mitochondria, Liver/enzymology Neoplasms, Experimental/enzymology Nucleotidyltransferases/metabolism RNA Nucleotidyltransferases/isolation & purification Rats Ribonucleases/pharmacology Tritium Uracil Nucleotides/metabolism
Chemicals
Cytosine Nucleotides Uracil Nucleotides Tritium Guanosine Triphosphate Adenosine Triphosphate Nucleotidyltransferases RNA Nucleotidyltransferases Ribonucleases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Jacob S T
Schindler D G
Morris H P
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1972-11-10
Pages
639-40
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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