Comparison of the ribonucleotide with the canavanine reductase system
Autor: | Masahide Sasaki, Arnold L. Schultz, Samuel Natelson |
---|---|
Rok vydání: | 1974 |
Předmět: |
Ribonucleotide
Carcinoma Hepatocellular Iron Reductase Biology Hydroxylamines General Biochemistry Genetics and Molecular Biology Dithiothreitol chemistry.chemical_compound Canavanine Ribonucleotide Reductases Animals Hydroxyurea Transplantation Homologous Cysteine Sulfhydryl Compounds Cells Cultured Edetic Acid chemistry.chemical_classification Thioctic Acid Liver Neoplasms Transferrin Succinates Glutathione Neoplasms Experimental Rats Ribonucleotide reductase chemistry Biochemistry Dimercaprol Female Amino Acid Oxidoreductases Oxidation-Reduction Cell Division Neoplasm Transplantation |
Zdroj: | Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.). 145(3) |
ISSN: | 0037-9727 |
Popis: | SummaryReduced lipoate and dithiothreitol act as hydrogen donors in the canavanine and ribonucleotide reductase systems. Other thiol derivatives such as cysteine, 2,3-dimercapto-1-propanol (BAL), and glutathione cannot substitute effectively for the lipoate or dithiothreitol. Fe2+ acts as a cofactor for both systems. The canavanine system is inhibited quantitatively by transferrin or BAL. Transferrin in sixfold excess will only inhibit the ribonucleotide reductase system by approximately 50%. BAL is a strong inhibitor of the ribonucleotide reductase system. Addition of excess Fe2+ does not remove all of the inhibition produced by BAL in the ribonucleotide reductase system. BAL administered subcutaneously to rats before and after intraperitoneal inoculation with hepatoma cells did not prevent the proliferation of the hepatoma cells.Supported in part by USPHS Grant AM 09958 and the Morris Natelson Research Fund.The authors wish to acknowledge assistance of E. Colleen Moore for some of the enzyme preparation... |
Databáze: | OpenAIRE |
Externí odkaz: |