Activation of 3-methyl-branched fatty acids in rat liver
1. 1. Subcellular fractionation of rat liver revealed that 3-methylmargaric acid, a monobranched phytanic acid analogue, can be activated by mitochondria, endoplasmic reticulum and peroxisomes. 2. 2. Indirect data (effects of pyrophosphate and Triton X-100) suggested that the peroxisomal activation...
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| Veröffentlicht in: | International journal of biochemistry 1994-09, Vol.26 (9), p.1095-1101 |
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| container_issue | 9 |
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| container_title | International journal of biochemistry |
| container_volume | 26 |
| creator | Vanhooren, J.C.T. Asselberghs, S. Eyssen, H.J. Mannaerts, G.P. Van Veldhoven, P.P. |
| description | 1.
1. Subcellular fractionation of rat liver revealed that 3-methylmargaric acid, a monobranched phytanic acid analogue, can be activated by mitochondria, endoplasmic reticulum and peroxisomes.
2.
2. Indirect data (effects of pyrophosphate and Triton X-100) suggested that the peroxisomal activation of 3-methylmargaric, 2-methylpalmitic and palmitic acid is catalyzed by different enzymes.
3.
3. Despite many attempts, column chromatography of solubilized peroxisomal membrane proteins so far did not provide more conclusive data. On various matrices, lignoceroyl-CoA synthetase clearly eluted differently from the synthetases acting on 3-methylmargaric, 2-methylpalmitic and palmitic acid. The latter three however, tended to coelute together, although often not in an identical manner. |
| doi_str_mv | 10.1016/0020-711X(94)90131-7 |
| format | Article |
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1. Subcellular fractionation of rat liver revealed that 3-methylmargaric acid, a monobranched phytanic acid analogue, can be activated by mitochondria, endoplasmic reticulum and peroxisomes.
2.
2. Indirect data (effects of pyrophosphate and Triton X-100) suggested that the peroxisomal activation of 3-methylmargaric, 2-methylpalmitic and palmitic acid is catalyzed by different enzymes.
3.
3. Despite many attempts, column chromatography of solubilized peroxisomal membrane proteins so far did not provide more conclusive data. On various matrices, lignoceroyl-CoA synthetase clearly eluted differently from the synthetases acting on 3-methylmargaric, 2-methylpalmitic and palmitic acid. The latter three however, tended to coelute together, although often not in an identical manner.</description><identifier>ISSN: 0020-711X</identifier><identifier>DOI: 10.1016/0020-711X(94)90131-7</identifier><identifier>PMID: 7988734</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Catalysis ; Cell Fractionation ; Centrifugation, Density Gradient ; Coenzyme A Ligases - metabolism ; Endoplasmic Reticulum - metabolism ; Fatty Acids - metabolism ; Liver - metabolism ; Liver - ultrastructure ; Male ; Microbodies - metabolism ; Mitochondria, Liver - metabolism ; Octoxynol - chemistry ; Palmitic Acid ; Palmitic Acids - metabolism ; Rats ; Rats, Wistar ; Repressor Proteins ; Saccharomyces cerevisiae Proteins</subject><ispartof>International journal of biochemistry, 1994-09, Vol.26 (9), p.1095-1101</ispartof><rights>1994</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c408t-1d7dc18e344a8073b24481d8cf8176c8ab6a5a235caa397c127666b81a7515553</citedby><cites>FETCH-LOGICAL-c408t-1d7dc18e344a8073b24481d8cf8176c8ab6a5a235caa397c127666b81a7515553</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7988734$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vanhooren, J.C.T.</creatorcontrib><creatorcontrib>Asselberghs, S.</creatorcontrib><creatorcontrib>Eyssen, H.J.</creatorcontrib><creatorcontrib>Mannaerts, G.P.</creatorcontrib><creatorcontrib>Van Veldhoven, P.P.</creatorcontrib><title>Activation of 3-methyl-branched fatty acids in rat liver</title><title>International journal of biochemistry</title><addtitle>Int J Biochem</addtitle><description>1.
1. Subcellular fractionation of rat liver revealed that 3-methylmargaric acid, a monobranched phytanic acid analogue, can be activated by mitochondria, endoplasmic reticulum and peroxisomes.
2.
2. Indirect data (effects of pyrophosphate and Triton X-100) suggested that the peroxisomal activation of 3-methylmargaric, 2-methylpalmitic and palmitic acid is catalyzed by different enzymes.
3.
3. Despite many attempts, column chromatography of solubilized peroxisomal membrane proteins so far did not provide more conclusive data. On various matrices, lignoceroyl-CoA synthetase clearly eluted differently from the synthetases acting on 3-methylmargaric, 2-methylpalmitic and palmitic acid. The latter three however, tended to coelute together, although often not in an identical manner.</description><subject>Animals</subject><subject>Catalysis</subject><subject>Cell Fractionation</subject><subject>Centrifugation, Density Gradient</subject><subject>Coenzyme A Ligases - metabolism</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Fatty Acids - metabolism</subject><subject>Liver - metabolism</subject><subject>Liver - ultrastructure</subject><subject>Male</subject><subject>Microbodies - metabolism</subject><subject>Mitochondria, Liver - metabolism</subject><subject>Octoxynol - chemistry</subject><subject>Palmitic Acid</subject><subject>Palmitic Acids - metabolism</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Repressor Proteins</subject><subject>Saccharomyces cerevisiae Proteins</subject><issn>0020-711X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLAzEQx3NQaq1-A4U9iR5WM5vsJnsRSvEFBS8K3kI2maWRfdQkLfTbu2tLj54G5v8Y5kfIFdB7oFA8UJrRVAB83Zb8rqTAIBUnZHpcn5HzEL4phVJymJCJKKUUjE-JnJvotjq6vkv6OmFpi3G1a9LK686s0Ca1jnGXaONsSFyXeB2Txm3RX5DTWjcBLw9zRj6fnz4Wr-ny_eVtMV-mhlMZU7DCGpDIONeSClZlnEuw0tQSRGGkrgqd64zlRmtWCgOZKIqikqBFDnmesxm52feuff-zwRBV64LBptEd9pugRCGHB0sxGPneaHwfgsdarb1rtd8poGqEpEYaaqShSq7-IKkxdn3o31Qt2mPoQGjQH_c6Dk9uHXoVjMPOoHUeTVS2d_8f-AUBa3Zt</recordid><startdate>19940901</startdate><enddate>19940901</enddate><creator>Vanhooren, J.C.T.</creator><creator>Asselberghs, S.</creator><creator>Eyssen, H.J.</creator><creator>Mannaerts, G.P.</creator><creator>Van Veldhoven, P.P.</creator><general>Elsevier B.V</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>19940901</creationdate><title>Activation of 3-methyl-branched fatty acids in rat liver</title><author>Vanhooren, J.C.T. ; Asselberghs, S. ; Eyssen, H.J. ; Mannaerts, G.P. ; Van Veldhoven, P.P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c408t-1d7dc18e344a8073b24481d8cf8176c8ab6a5a235caa397c127666b81a7515553</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Catalysis</topic><topic>Cell Fractionation</topic><topic>Centrifugation, Density Gradient</topic><topic>Coenzyme A Ligases - metabolism</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Fatty Acids - metabolism</topic><topic>Liver - metabolism</topic><topic>Liver - ultrastructure</topic><topic>Male</topic><topic>Microbodies - metabolism</topic><topic>Mitochondria, Liver - metabolism</topic><topic>Octoxynol - chemistry</topic><topic>Palmitic Acid</topic><topic>Palmitic Acids - metabolism</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Repressor Proteins</topic><topic>Saccharomyces cerevisiae Proteins</topic><toplevel>online_resources</toplevel><creatorcontrib>Vanhooren, J.C.T.</creatorcontrib><creatorcontrib>Asselberghs, S.</creatorcontrib><creatorcontrib>Eyssen, H.J.</creatorcontrib><creatorcontrib>Mannaerts, G.P.</creatorcontrib><creatorcontrib>Van Veldhoven, P.P.</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>International journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vanhooren, J.C.T.</au><au>Asselberghs, S.</au><au>Eyssen, H.J.</au><au>Mannaerts, G.P.</au><au>Van Veldhoven, P.P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of 3-methyl-branched fatty acids in rat liver</atitle><jtitle>International journal of biochemistry</jtitle><addtitle>Int J Biochem</addtitle><date>1994-09-01</date><risdate>1994</risdate><volume>26</volume><issue>9</issue><spage>1095</spage><epage>1101</epage><pages>1095-1101</pages><issn>0020-711X</issn><abstract>1.
1. Subcellular fractionation of rat liver revealed that 3-methylmargaric acid, a monobranched phytanic acid analogue, can be activated by mitochondria, endoplasmic reticulum and peroxisomes.
2.
2. Indirect data (effects of pyrophosphate and Triton X-100) suggested that the peroxisomal activation of 3-methylmargaric, 2-methylpalmitic and palmitic acid is catalyzed by different enzymes.
3.
3. Despite many attempts, column chromatography of solubilized peroxisomal membrane proteins so far did not provide more conclusive data. On various matrices, lignoceroyl-CoA synthetase clearly eluted differently from the synthetases acting on 3-methylmargaric, 2-methylpalmitic and palmitic acid. The latter three however, tended to coelute together, although often not in an identical manner.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>7988734</pmid><doi>10.1016/0020-711X(94)90131-7</doi><tpages>7</tpages></addata></record> |
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| ispartof | International journal of biochemistry, 1994-09, Vol.26 (9), p.1095-1101 |
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| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Animals Catalysis Cell Fractionation Centrifugation, Density Gradient Coenzyme A Ligases - metabolism Endoplasmic Reticulum - metabolism Fatty Acids - metabolism Liver - metabolism Liver - ultrastructure Male Microbodies - metabolism Mitochondria, Liver - metabolism Octoxynol - chemistry Palmitic Acid Palmitic Acids - metabolism Rats Rats, Wistar Repressor Proteins Saccharomyces cerevisiae Proteins |
| title | Activation of 3-methyl-branched fatty acids in rat liver |
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