Subcellular Distribution of Branched-Chain Aminotransferase Activity in Rat Tissues
The activity of branched-chain aminotransferase in mitochondria isolated from rat tissues was examined, and the mitochondrial contribution to total tissue branched-chain aminotransferase activity was calculated using the mitochondrial marker enzyme citrate synthase. Mitochondrial aminotransferase ac...
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| Veröffentlicht in: | The Journal of nutrition 1988-12, Vol.118 (12), p.1475-1481 |
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| creator | Hutson, Susan M. |
| description | The activity of branched-chain aminotransferase in mitochondria isolated from rat tissues was examined, and the mitochondrial contribution to total tissue branched-chain aminotransferase activity was calculated using the mitochondrial marker enzyme citrate synthase. Mitochondrial aminotransferase activity was highest in heart followed by skeletal muscle, kidney and brain. In heart muscle all of the aminotransferase activity was accounted for by the mitochondrial fraction. Activity was found to be mitochondrial in skeletal muscle with high red fiber content and also in kidney cortex. Activity was predominantly cytosolic in brain and muscles with high white fiber composition. Thus, the distribution of branched-chain aminotransferase activity in skeletal muscle was dependent on fiber type. No branched-chain aminotransferase activity was detected in liver mitochondria, and in liver tissue activity was too low to be relevant at physiological concentrations of branched-chain amino acids. Within a tissue, regardless of the subcellular distribution of aminotransferase activity, the relative rates of transamination with subsaturating or “saturating” concentrations of KIV or isoleucine were similar. Finally, amino acid preference was also similar within a tissue, but not necessarily between or among different tissues. |
| doi_str_mv | 10.1093/jn/118.12.1475 |
| format | Article |
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Mitochondrial aminotransferase activity was highest in heart followed by skeletal muscle, kidney and brain. In heart muscle all of the aminotransferase activity was accounted for by the mitochondrial fraction. Activity was found to be mitochondrial in skeletal muscle with high red fiber content and also in kidney cortex. Activity was predominantly cytosolic in brain and muscles with high white fiber composition. Thus, the distribution of branched-chain aminotransferase activity in skeletal muscle was dependent on fiber type. No branched-chain aminotransferase activity was detected in liver mitochondria, and in liver tissue activity was too low to be relevant at physiological concentrations of branched-chain amino acids. Within a tissue, regardless of the subcellular distribution of aminotransferase activity, the relative rates of transamination with subsaturating or “saturating” concentrations of KIV or isoleucine were similar. Finally, amino acid preference was also similar within a tissue, but not necessarily between or among different tissues.</description><identifier>ISSN: 0022-3166</identifier><identifier>EISSN: 1541-6100</identifier><identifier>DOI: 10.1093/jn/118.12.1475</identifier><identifier>PMID: 3210076</identifier><identifier>CODEN: JONUAI</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>ACIDE AMINE ; AMINOACIDOS ; Animals ; Biological and medical sciences ; Brain - enzymology ; branched-chain amino acids ; branched-chain aminotransferase ; Citrate (si)-Synthase - analysis ; Cytosol - enzymology ; Enzymes. Coenzymes. Vitamins. Pigments ; Fundamental and applied biological sciences. Psychology ; Kidney Cortex - enzymology ; Male ; Metabolisms and neurohumoral controls ; Mitochondria - enzymology ; Mitochondria, Heart - enzymology ; Mitochondria, Liver - enzymology ; mitochondrial transamination ; MITOCHONDRIE ; MITOCONDRIA ; Muscles - enzymology ; RAT ; RATA ; Rats ; Rats, Inbred Strains ; Subcellular Fractions - enzymology ; TEJIDO (ANATOMIA) ; TISSU ; TRANSAMINACION ; Transaminases - analysis ; TRANSAMINATION ; TRANSFERASAS ; TRANSFERASE ; Vertebrates: anatomy and physiology, studies on body, several organs or systems</subject><ispartof>The Journal of nutrition, 1988-12, Vol.118 (12), p.1475-1481</ispartof><rights>1988 American Society for Nutrition.</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c493t-69a9da91f213569bf8723be59031f0461df3718c12d859c8acc51aab55c08ddf3</citedby><cites>FETCH-LOGICAL-c493t-69a9da91f213569bf8723be59031f0461df3718c12d859c8acc51aab55c08ddf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7159993$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3210076$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hutson, Susan M.</creatorcontrib><title>Subcellular Distribution of Branched-Chain Aminotransferase Activity in Rat Tissues</title><title>The Journal of nutrition</title><addtitle>J Nutr</addtitle><description>The activity of branched-chain aminotransferase in mitochondria isolated from rat tissues was examined, and the mitochondrial contribution to total tissue branched-chain aminotransferase activity was calculated using the mitochondrial marker enzyme citrate synthase. Mitochondrial aminotransferase activity was highest in heart followed by skeletal muscle, kidney and brain. In heart muscle all of the aminotransferase activity was accounted for by the mitochondrial fraction. Activity was found to be mitochondrial in skeletal muscle with high red fiber content and also in kidney cortex. Activity was predominantly cytosolic in brain and muscles with high white fiber composition. Thus, the distribution of branched-chain aminotransferase activity in skeletal muscle was dependent on fiber type. No branched-chain aminotransferase activity was detected in liver mitochondria, and in liver tissue activity was too low to be relevant at physiological concentrations of branched-chain amino acids. Within a tissue, regardless of the subcellular distribution of aminotransferase activity, the relative rates of transamination with subsaturating or “saturating” concentrations of KIV or isoleucine were similar. Finally, amino acid preference was also similar within a tissue, but not necessarily between or among different tissues.</description><subject>ACIDE AMINE</subject><subject>AMINOACIDOS</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Brain - enzymology</subject><subject>branched-chain amino acids</subject><subject>branched-chain aminotransferase</subject><subject>Citrate (si)-Synthase - analysis</subject><subject>Cytosol - enzymology</subject><subject>Enzymes. Coenzymes. Vitamins. Pigments</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kidney Cortex - enzymology</subject><subject>Male</subject><subject>Metabolisms and neurohumoral controls</subject><subject>Mitochondria - enzymology</subject><subject>Mitochondria, Heart - enzymology</subject><subject>Mitochondria, Liver - enzymology</subject><subject>mitochondrial transamination</subject><subject>MITOCHONDRIE</subject><subject>MITOCONDRIA</subject><subject>Muscles - enzymology</subject><subject>RAT</subject><subject>RATA</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Subcellular Fractions - enzymology</subject><subject>TEJIDO (ANATOMIA)</subject><subject>TISSU</subject><subject>TRANSAMINACION</subject><subject>Transaminases - analysis</subject><subject>TRANSAMINATION</subject><subject>TRANSFERASAS</subject><subject>TRANSFERASE</subject><subject>Vertebrates: anatomy and physiology, studies on body, several organs or systems</subject><issn>0022-3166</issn><issn>1541-6100</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1r3DAQQEVpSbdprz0UCj6U3ryZkSxbOm62nxAodJOzGMtSo8Vrp5IcyL-vll1y60mg90Yfj7H3CGsELa720xWiWiNfY9PJF2yFssG6RYCXbAXAeS2wbV-zNyntAQAbrS7YheBF6NoV2-2W3rpxXEaK1ZeQcgz9ksM8VbOvriNN9t4N9faewlRtDmGac9lL3kVKrtrYHB5DfqoK_E25ug0pLS69Za88jcm9O6-X7O7b19vtj_rm1_ef281NbRstct1q0gNp9ByFbHXvVcdF76QGgR6aFgcvOlQW-aCktoqslUjUS2lBDQVess-ncx_i_Lfcm80hpONnaHLzkkxXxkBLKOL6JNo4pxSdNw8xHCg-GQRzrGj2kykVDXJzrFgGPp5PXvqDG571c7bCP505JUujP3YK6VnrUGqtRdE-nDRPs6E_sSh3O6Wh4dAVqE7QlUSPwUWTbHCTdUOIzmYzzOF_z_sHv7KVMg</recordid><startdate>19881201</startdate><enddate>19881201</enddate><creator>Hutson, Susan M.</creator><general>Elsevier Inc</general><general>American Society for Nutritional Sciences</general><scope>FBQ</scope><scope>IQODW</scope><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>19881201</creationdate><title>Subcellular Distribution of Branched-Chain Aminotransferase Activity in Rat Tissues</title><author>Hutson, Susan M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c493t-69a9da91f213569bf8723be59031f0461df3718c12d859c8acc51aab55c08ddf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>ACIDE AMINE</topic><topic>AMINOACIDOS</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Brain - enzymology</topic><topic>branched-chain amino acids</topic><topic>branched-chain aminotransferase</topic><topic>Citrate (si)-Synthase - analysis</topic><topic>Cytosol - enzymology</topic><topic>Enzymes. Coenzymes. Vitamins. Pigments</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kidney Cortex - enzymology</topic><topic>Male</topic><topic>Metabolisms and neurohumoral controls</topic><topic>Mitochondria - enzymology</topic><topic>Mitochondria, Heart - enzymology</topic><topic>Mitochondria, Liver - enzymology</topic><topic>mitochondrial transamination</topic><topic>MITOCHONDRIE</topic><topic>MITOCONDRIA</topic><topic>Muscles - enzymology</topic><topic>RAT</topic><topic>RATA</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Subcellular Fractions - enzymology</topic><topic>TEJIDO (ANATOMIA)</topic><topic>TISSU</topic><topic>TRANSAMINACION</topic><topic>Transaminases - analysis</topic><topic>TRANSAMINATION</topic><topic>TRANSFERASAS</topic><topic>TRANSFERASE</topic><topic>Vertebrates: anatomy and physiology, studies on body, several organs or systems</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hutson, Susan M.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><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>The Journal of nutrition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hutson, Susan M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Subcellular Distribution of Branched-Chain Aminotransferase Activity in Rat Tissues</atitle><jtitle>The Journal of nutrition</jtitle><addtitle>J Nutr</addtitle><date>1988-12-01</date><risdate>1988</risdate><volume>118</volume><issue>12</issue><spage>1475</spage><epage>1481</epage><pages>1475-1481</pages><issn>0022-3166</issn><eissn>1541-6100</eissn><coden>JONUAI</coden><abstract>The activity of branched-chain aminotransferase in mitochondria isolated from rat tissues was examined, and the mitochondrial contribution to total tissue branched-chain aminotransferase activity was calculated using the mitochondrial marker enzyme citrate synthase. Mitochondrial aminotransferase activity was highest in heart followed by skeletal muscle, kidney and brain. In heart muscle all of the aminotransferase activity was accounted for by the mitochondrial fraction. Activity was found to be mitochondrial in skeletal muscle with high red fiber content and also in kidney cortex. Activity was predominantly cytosolic in brain and muscles with high white fiber composition. Thus, the distribution of branched-chain aminotransferase activity in skeletal muscle was dependent on fiber type. No branched-chain aminotransferase activity was detected in liver mitochondria, and in liver tissue activity was too low to be relevant at physiological concentrations of branched-chain amino acids. Within a tissue, regardless of the subcellular distribution of aminotransferase activity, the relative rates of transamination with subsaturating or “saturating” concentrations of KIV or isoleucine were similar. Finally, amino acid preference was also similar within a tissue, but not necessarily between or among different tissues.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>3210076</pmid><doi>10.1093/jn/118.12.1475</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | ACIDE AMINE AMINOACIDOS Animals Biological and medical sciences Brain - enzymology branched-chain amino acids branched-chain aminotransferase Citrate (si)-Synthase - analysis Cytosol - enzymology Enzymes. Coenzymes. Vitamins. Pigments Fundamental and applied biological sciences. Psychology Kidney Cortex - enzymology Male Metabolisms and neurohumoral controls Mitochondria - enzymology Mitochondria, Heart - enzymology Mitochondria, Liver - enzymology mitochondrial transamination MITOCHONDRIE MITOCONDRIA Muscles - enzymology RAT RATA Rats Rats, Inbred Strains Subcellular Fractions - enzymology TEJIDO (ANATOMIA) TISSU TRANSAMINACION Transaminases - analysis TRANSAMINATION TRANSFERASAS TRANSFERASE Vertebrates: anatomy and physiology, studies on body, several organs or systems |
| title | Subcellular Distribution of Branched-Chain Aminotransferase Activity in Rat Tissues |
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