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Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells
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Zeitschriftentitel: | Journal of Cellular Physiology |
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Personen und Körperschaften: | , , , , |
In: | Journal of Cellular Physiology, 93, 1977, 3, S. 345-352 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Wiley
|
Schlagwörter: |
author_facet |
Lewis, William H. McNaughton, David R. Goh, Swee Han Lejohn, Herb B. Wright, Jim A. Lewis, William H. McNaughton, David R. Goh, Swee Han Lejohn, Herb B. Wright, Jim A. |
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author |
Lewis, William H. McNaughton, David R. Goh, Swee Han Lejohn, Herb B. Wright, Jim A. |
spellingShingle |
Lewis, William H. McNaughton, David R. Goh, Swee Han Lejohn, Herb B. Wright, Jim A. Journal of Cellular Physiology Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells Cell Biology Clinical Biochemistry Physiology |
author_sort |
lewis, william h. |
spelling |
Lewis, William H. McNaughton, David R. Goh, Swee Han Lejohn, Herb B. Wright, Jim A. 0021-9541 1097-4652 Wiley Cell Biology Clinical Biochemistry Physiology http://dx.doi.org/10.1002/jcp.1040930305 <jats:title>Abstract</jats:title><jats:p>HS3, a highly phosphorylated dinucleoside originally purified from the fungus <jats:italic>Achlya</jats:italic>, has been isolated from Chinese hamster ovary cells undergoing glutamine starvation. The HS3 compounds obtained from the fungal and mammalian sources exhibited similar physical and chemical properties. This unusual dinucleotide may be an important regulator of eucaryotic ribonucleoside diphosphate reductase activity; for 50 μm HS3, isolated from either mammalian or fungal cells, significantly inhibited CDP reduction in <jats:italic>Achlya</jats:italic> or hamster cell preparations, but only marginally affected the activity of the enzyme from <jats:italic>E</jats:italic>. <jats:italic>coli</jats:italic>. Studies with HS3 isolated from <jats:italic>Achlya</jats:italic> and partially purified mammalian ribonucleotide reductase indicated that the compound noncompetitively inhibited the reduction of varying concentrations of the substrates CDP, ADP and GDP with Ki values of 23 μm, 14 μM and 16 μM respectively. These inhibitor concentrations are well below the estimated intracellular levels of HS3 in glutamine starved cells and suggest that HS3 inhibition of ribonucleotide reduction may be responsible for the rapid inhibition of DNA synthesis seen under these culture conditions.</jats:p> Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells Journal of Cellular Physiology |
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10.1002/jcp.1040930305 |
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1977 |
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Wiley |
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Journal of Cellular Physiology |
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title |
Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
title_unstemmed |
Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
title_full |
Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
title_fullStr |
Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
title_full_unstemmed |
Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
title_short |
Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
title_sort |
inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
topic |
Cell Biology Clinical Biochemistry Physiology |
url |
http://dx.doi.org/10.1002/jcp.1040930305 |
publishDate |
1977 |
physical |
345-352 |
description |
<jats:title>Abstract</jats:title><jats:p>HS3, a highly phosphorylated dinucleoside originally purified from the fungus <jats:italic>Achlya</jats:italic>, has been isolated from Chinese hamster ovary cells undergoing glutamine starvation. The HS3 compounds obtained from the fungal and mammalian sources exhibited similar physical and chemical properties. This unusual dinucleotide may be an important regulator of eucaryotic ribonucleoside diphosphate reductase activity; for 50 μm HS3, isolated from either mammalian or fungal cells, significantly inhibited CDP reduction in <jats:italic>Achlya</jats:italic> or hamster cell preparations, but only marginally affected the activity of the enzyme from <jats:italic>E</jats:italic>. <jats:italic>coli</jats:italic>. Studies with HS3 isolated from <jats:italic>Achlya</jats:italic> and partially purified mammalian ribonucleotide reductase indicated that the compound noncompetitively inhibited the reduction of varying concentrations of the substrates CDP, ADP and GDP with Ki values of 23 μm, 14 μM and 16 μM respectively. These inhibitor concentrations are well below the estimated intracellular levels of HS3 in glutamine starved cells and suggest that HS3 inhibition of ribonucleotide reduction may be responsible for the rapid inhibition of DNA synthesis seen under these culture conditions.</jats:p> |
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author | Lewis, William H., McNaughton, David R., Goh, Swee Han, Lejohn, Herb B., Wright, Jim A. |
author_facet | Lewis, William H., McNaughton, David R., Goh, Swee Han, Lejohn, Herb B., Wright, Jim A., Lewis, William H., McNaughton, David R., Goh, Swee Han, Lejohn, Herb B., Wright, Jim A. |
author_sort | lewis, william h. |
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container_title | Journal of Cellular Physiology |
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description | <jats:title>Abstract</jats:title><jats:p>HS3, a highly phosphorylated dinucleoside originally purified from the fungus <jats:italic>Achlya</jats:italic>, has been isolated from Chinese hamster ovary cells undergoing glutamine starvation. The HS3 compounds obtained from the fungal and mammalian sources exhibited similar physical and chemical properties. This unusual dinucleotide may be an important regulator of eucaryotic ribonucleoside diphosphate reductase activity; for 50 μm HS3, isolated from either mammalian or fungal cells, significantly inhibited CDP reduction in <jats:italic>Achlya</jats:italic> or hamster cell preparations, but only marginally affected the activity of the enzyme from <jats:italic>E</jats:italic>. <jats:italic>coli</jats:italic>. Studies with HS3 isolated from <jats:italic>Achlya</jats:italic> and partially purified mammalian ribonucleotide reductase indicated that the compound noncompetitively inhibited the reduction of varying concentrations of the substrates CDP, ADP and GDP with Ki values of 23 μm, 14 μM and 16 μM respectively. These inhibitor concentrations are well below the estimated intracellular levels of HS3 in glutamine starved cells and suggest that HS3 inhibition of ribonucleotide reduction may be responsible for the rapid inhibition of DNA synthesis seen under these culture conditions.</jats:p> |
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imprint | Wiley, 1977 |
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spelling | Lewis, William H. McNaughton, David R. Goh, Swee Han Lejohn, Herb B. Wright, Jim A. 0021-9541 1097-4652 Wiley Cell Biology Clinical Biochemistry Physiology http://dx.doi.org/10.1002/jcp.1040930305 <jats:title>Abstract</jats:title><jats:p>HS3, a highly phosphorylated dinucleoside originally purified from the fungus <jats:italic>Achlya</jats:italic>, has been isolated from Chinese hamster ovary cells undergoing glutamine starvation. The HS3 compounds obtained from the fungal and mammalian sources exhibited similar physical and chemical properties. This unusual dinucleotide may be an important regulator of eucaryotic ribonucleoside diphosphate reductase activity; for 50 μm HS3, isolated from either mammalian or fungal cells, significantly inhibited CDP reduction in <jats:italic>Achlya</jats:italic> or hamster cell preparations, but only marginally affected the activity of the enzyme from <jats:italic>E</jats:italic>. <jats:italic>coli</jats:italic>. Studies with HS3 isolated from <jats:italic>Achlya</jats:italic> and partially purified mammalian ribonucleotide reductase indicated that the compound noncompetitively inhibited the reduction of varying concentrations of the substrates CDP, ADP and GDP with Ki values of 23 μm, 14 μM and 16 μM respectively. These inhibitor concentrations are well below the estimated intracellular levels of HS3 in glutamine starved cells and suggest that HS3 inhibition of ribonucleotide reduction may be responsible for the rapid inhibition of DNA synthesis seen under these culture conditions.</jats:p> Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells Journal of Cellular Physiology |
spellingShingle | Lewis, William H., McNaughton, David R., Goh, Swee Han, Lejohn, Herb B., Wright, Jim A., Journal of Cellular Physiology, Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells, Cell Biology, Clinical Biochemistry, Physiology |
title | Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
title_full | Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
title_fullStr | Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
title_full_unstemmed | Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
title_short | Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
title_sort | inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
title_unstemmed | Inhibition of mammalian ribonucleotide reductase by a dinucleotide produced in eucaryotic cells |
topic | Cell Biology, Clinical Biochemistry, Physiology |
url | http://dx.doi.org/10.1002/jcp.1040930305 |