The ATP-dependent reductive carboxylation of 2-oxoglutarate using cytosol from rat liver
An enzyme system (isocitrate synthase) catalysing the conversion of 2-oxoglutarate to isocitrate has been detected in and partially purified from rat liver. The activity of this enzyme system is dependent on the presence of Mg 2+, ATP, HCO 3 − and NADPH. The major proportion of the isocitrate syntha...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1976-08, Vol.71 (3), p.712-718 |
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| container_issue | 3 |
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| container_title | Biochemical and biophysical research communications |
| container_volume | 71 |
| creator | Keech, D.Bruce Mattoo, Autar K. Carabott, Mary J.J. Wallace, John C. |
| description | An enzyme system (isocitrate synthase) catalysing the conversion of 2-oxoglutarate to isocitrate has been detected in and partially purified from rat liver. The activity of this enzyme system is dependent on the presence of Mg
2+, ATP,
HCO
3
−
and NADPH.
The major proportion of the isocitrate synthase was found in the cytosol and its level of activity was related to the nutritional state of the animal, undergoing changes parallel to those observed in the rate of lipogenesis. During purification, the activity of the isocitrate synthase system increased relative to that of isocitrate dehydrogenase (NADP
+). |
| doi_str_mv | 10.1016/0006-291X(76)90889-5 |
| format | Article |
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2+, ATP,
HCO
3
−
and NADPH.
The major proportion of the isocitrate synthase was found in the cytosol and its level of activity was related to the nutritional state of the animal, undergoing changes parallel to those observed in the rate of lipogenesis. During purification, the activity of the isocitrate synthase system increased relative to that of isocitrate dehydrogenase (NADP
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2+, ATP,
HCO
3
−
and NADPH.
The major proportion of the isocitrate synthase was found in the cytosol and its level of activity was related to the nutritional state of the animal, undergoing changes parallel to those observed in the rate of lipogenesis. During purification, the activity of the isocitrate synthase system increased relative to that of isocitrate dehydrogenase (NADP
+).</description><subject>Adenosine Triphosphate - pharmacology</subject><subject>Animals</subject><subject>Cytosol - drug effects</subject><subject>Cytosol - enzymology</subject><subject>Enzyme Activation - drug effects</subject><subject>Isocitrate Dehydrogenase - isolation & purification</subject><subject>Isocitrate Dehydrogenase - metabolism</subject><subject>Liver - enzymology</subject><subject>Magnesium - pharmacology</subject><subject>Multienzyme Complexes - metabolism</subject><subject>NAD</subject><subject>Rats</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtKJDEUhsOgo60zb-AiK3EWpTmpS6o2QiOOCoKzaMFdyOVEI9WVNkmJ_fZTbYvuXB34b3A-Qo6AnQKD5owx1hS8g4cT0fzpWNt2Rf2DzIB1rODAqh0y-4zsk4OUnhkDqJpuj_yEthSim5GHxRPS-eJfYXGFg8Uh04h2NNm_IjUq6vC27lX2YaDBUV6Et_DYj1lFlZGOyQ-P1KxzSKGnLoYlnXTaT934i-w61Sf8_XEPyf3fy8XFdXF7d3VzMb8tTFk3udColQMNYLS2gmtV1dYoCwJBtzVWphUlZ6q0ldOIgIJxx4UxrXOuEuDKQ3K83V3F8DJiynLpk8G-VwOGMcm2rDkvmZiC1TZoYkgpopOr6JcqriUwueEpN7DkBpYUjXznKeupdvSxP-ol2q_SO8DJPt_aOP346jHKZDwOBq2PaLK0wX-__x90_oc2</recordid><startdate>19760809</startdate><enddate>19760809</enddate><creator>Keech, D.Bruce</creator><creator>Mattoo, Autar K.</creator><creator>Carabott, Mary J.J.</creator><creator>Wallace, John C.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19760809</creationdate><title>The ATP-dependent reductive carboxylation of 2-oxoglutarate using cytosol from rat liver</title><author>Keech, D.Bruce ; Mattoo, Autar K. ; Carabott, Mary J.J. ; Wallace, John C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-bebaf1b11cbbd72ba45dcad17e1b85e4c87320a3d4fbee1e702f27cc8fff471f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Adenosine Triphosphate - pharmacology</topic><topic>Animals</topic><topic>Cytosol - drug effects</topic><topic>Cytosol - enzymology</topic><topic>Enzyme Activation - drug effects</topic><topic>Isocitrate Dehydrogenase - isolation & purification</topic><topic>Isocitrate Dehydrogenase - metabolism</topic><topic>Liver - enzymology</topic><topic>Magnesium - pharmacology</topic><topic>Multienzyme Complexes - metabolism</topic><topic>NAD</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Keech, D.Bruce</creatorcontrib><creatorcontrib>Mattoo, Autar K.</creatorcontrib><creatorcontrib>Carabott, Mary J.J.</creatorcontrib><creatorcontrib>Wallace, John C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Keech, D.Bruce</au><au>Mattoo, Autar K.</au><au>Carabott, Mary J.J.</au><au>Wallace, John C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The ATP-dependent reductive carboxylation of 2-oxoglutarate using cytosol from rat liver</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1976-08-09</date><risdate>1976</risdate><volume>71</volume><issue>3</issue><spage>712</spage><epage>718</epage><pages>712-718</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>An enzyme system (isocitrate synthase) catalysing the conversion of 2-oxoglutarate to isocitrate has been detected in and partially purified from rat liver. The activity of this enzyme system is dependent on the presence of Mg
2+, ATP,
HCO
3
−
and NADPH.
The major proportion of the isocitrate synthase was found in the cytosol and its level of activity was related to the nutritional state of the animal, undergoing changes parallel to those observed in the rate of lipogenesis. During purification, the activity of the isocitrate synthase system increased relative to that of isocitrate dehydrogenase (NADP
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| fulltext | fulltext |
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| ispartof | Biochemical and biophysical research communications, 1976-08, Vol.71 (3), p.712-718 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Adenosine Triphosphate - pharmacology Animals Cytosol - drug effects Cytosol - enzymology Enzyme Activation - drug effects Isocitrate Dehydrogenase - isolation & purification Isocitrate Dehydrogenase - metabolism Liver - enzymology Magnesium - pharmacology Multienzyme Complexes - metabolism NAD Rats |
| title | The ATP-dependent reductive carboxylation of 2-oxoglutarate using cytosol from rat liver |
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