[Some properties of cytoplasmic thymidine kinase and nucleoside phosphotransferase from rat liver].
Identifieur interne : 000888 ( Ncbi/Curation ); précédent : 000887; suivant : 000889[Some properties of cytoplasmic thymidine kinase and nucleoside phosphotransferase from rat liver].
Auteurs : S A Silaeva ; L V Isaeva ; A Ia NikolaevSource :
- Biokhimiia (Moscow, Russia) [ 0320-9725 ] ; 1977.
English descriptors
- KwdEn :
- Animals, Cytoplasm (enzymology), Deoxycytosine Nucleotides (pharmacology), Drug Stability, Fish Proteins, Hot Temperature, Isoenzymes (metabolism), Liver (enzymology), Liver Regeneration, Nucleosides, Phosphotransferases (antagonists & inhibitors), Phosphotransferases (metabolism), Protamines (pharmacology), Rats, Thymidine Kinase (antagonists & inhibitors), Thymidine Kinase (metabolism), Thymine Nucleotides (pharmacology).
- MESH :
- chemical , antagonists & inhibitors : Phosphotransferases, Thymidine Kinase.
- chemical , metabolism : Isoenzymes, Phosphotransferases, Thymidine Kinase.
- chemical , pharmacology : Deoxycytosine Nucleotides, Protamines, Thymine Nucleotides.
- enzymology : Cytoplasm, Liver.
- Animals, Drug Stability, Fish Proteins, Hot Temperature, Liver Regeneration, Nucleosides, Rats.
Abstract
The activities of two deoxythymidine-phosphorylating enzymes--thymidine kinase and nucleoside phosphotransferase--were found in the cytoplasmic fraction of normal and regenerating rat liver. The specific activity of nucleoside phosphotransferase appeared to be by 50% higher than that of thymidine kinase. Nucleoside phosphotransferase has a broad specificity for the phosphate donor. This enzyme is more stable to heating and prolonged dialysis as compared to thymidine kinase. The enzymes respond differently to the addition of d-TTP, d-CTP and sturins A and B: thymidine kinase is strongly inhibited by these agents whereas nucleoside phosphotransferase is insensitive to d-TTP and d-CTP and is only slightly inhibited by sturins. On the other hand the activity of nucleoside phosphotransferase is considerably decreased after addition of ATP. Changes in the activities of both enzymes during 50 hrs following partial hepatectomy were studied. Two activity maxima were observed at 20-22 and 40-46 hrs of regeneration. Using polyacrylamide gel electrophoresis, three isoforms of both enzymes were found. The ratio between the isoenzyme content of the two enzymes from the cytoplasmic fraction of regenerating liver varied as compared to normal.
PubMed: 911949
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pubmed:911949Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">[Some properties of cytoplasmic thymidine kinase and nucleoside phosphotransferase from rat liver].</title><author><name sortKey="Silaeva, S A" sort="Silaeva, S A" uniqKey="Silaeva S" first="S A" last="Silaeva">S A Silaeva</name></author><author><name sortKey="Isaeva, L V" sort="Isaeva, L V" uniqKey="Isaeva L" first="L V" last="Isaeva">L V Isaeva</name></author><author><name sortKey="Nikolaev, A Ia" sort="Nikolaev, A Ia" uniqKey="Nikolaev A" first="A Ia" last="Nikolaev">A Ia Nikolaev</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1977">1977</date><idno type="RBID">pubmed:911949</idno><idno type="pmid">911949</idno><idno type="wicri:Area/PubMed/Corpus">000813</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000813</idno><idno type="wicri:Area/PubMed/Curation">000813</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000813</idno><idno type="wicri:Area/PubMed/Checkpoint">000813</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000813</idno><idno type="wicri:Area/Ncbi/Merge">000888</idno><idno type="wicri:Area/Ncbi/Curation">000888</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">[Some properties of cytoplasmic thymidine kinase and nucleoside phosphotransferase from rat liver].</title><author><name sortKey="Silaeva, S A" sort="Silaeva, S A" uniqKey="Silaeva S" first="S A" last="Silaeva">S A Silaeva</name></author><author><name sortKey="Isaeva, L V" sort="Isaeva, L V" uniqKey="Isaeva L" first="L V" last="Isaeva">L V Isaeva</name></author><author><name sortKey="Nikolaev, A Ia" sort="Nikolaev, A Ia" uniqKey="Nikolaev A" first="A Ia" last="Nikolaev">A Ia Nikolaev</name></author></analytic><series><title level="j">Biokhimiia (Moscow, Russia)</title><idno type="ISSN">0320-9725</idno><imprint><date when="1977" type="published">1977</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cytoplasm (enzymology)</term><term>Deoxycytosine Nucleotides (pharmacology)</term><term>Drug Stability</term><term>Fish Proteins</term><term>Hot Temperature</term><term>Isoenzymes (metabolism)</term><term>Liver (enzymology)</term><term>Liver Regeneration</term><term>Nucleosides</term><term>Phosphotransferases (antagonists & inhibitors)</term><term>Phosphotransferases (metabolism)</term><term>Protamines (pharmacology)</term><term>Rats</term><term>Thymidine Kinase (antagonists & inhibitors)</term><term>Thymidine Kinase (metabolism)</term><term>Thymine Nucleotides (pharmacology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Phosphotransferases</term><term>Thymidine Kinase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Isoenzymes</term><term>Phosphotransferases</term><term>Thymidine Kinase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Deoxycytosine Nucleotides</term><term>Protamines</term><term>Thymine Nucleotides</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cytoplasm</term><term>Liver</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Drug Stability</term><term>Fish Proteins</term><term>Hot Temperature</term><term>Liver Regeneration</term><term>Nucleosides</term><term>Rats</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The activities of two deoxythymidine-phosphorylating enzymes--thymidine kinase and nucleoside phosphotransferase--were found in the cytoplasmic fraction of normal and regenerating rat liver. The specific activity of nucleoside phosphotransferase appeared to be by 50% higher than that of thymidine kinase. Nucleoside phosphotransferase has a broad specificity for the phosphate donor. This enzyme is more stable to heating and prolonged dialysis as compared to thymidine kinase. The enzymes respond differently to the addition of d-TTP, d-CTP and sturins A and B: thymidine kinase is strongly inhibited by these agents whereas nucleoside phosphotransferase is insensitive to d-TTP and d-CTP and is only slightly inhibited by sturins. On the other hand the activity of nucleoside phosphotransferase is considerably decreased after addition of ATP. Changes in the activities of both enzymes during 50 hrs following partial hepatectomy were studied. Two activity maxima were observed at 20-22 and 40-46 hrs of regeneration. Using polyacrylamide gel electrophoresis, three isoforms of both enzymes were found. The ratio between the isoenzyme content of the two enzymes from the cytoplasmic fraction of regenerating liver varied as compared to normal.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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