Modifications of Trout (Oncorhynchus mykiss) Muscle Proteins by Preslaughter Activity
The effect of two different preslaughter procedures (limited or 15-min intense muscular activity) on muscle trout proteins was investigated. Muscle was sampled 45 min and 24 h post-mortem, proteins were separated using two-dimensional electrophoresis, and spots of interest were tentatively identifie...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2006-04, Vol.54 (8), p.2997-3001 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Morzel, Martine Chambon, Christophe Lefèvre, Florence Paboeuf, Gilles Laville, Elisabeth |
| description | The effect of two different preslaughter procedures (limited or 15-min intense muscular activity) on muscle trout proteins was investigated. Muscle was sampled 45 min and 24 h post-mortem, proteins were separated using two-dimensional electrophoresis, and spots of interest were tentatively identified by MALDI-TOF spectrometry. Twenty-nine and 4 spots were differentially represented between the two groups of fish at 45 min and 24 h post-mortem, respectively. Spots that could be identified corresponded mainly to proteins involved in energy-producing pathways (triosephosphate isomerase, enolase, pyruvate dehydrogenase) or to structural proteins (desmin, cap-Z, myosin heavy chain fragment). Persistent under-representation of desmin, a key cytoskeletal protein, in fish submitted to intense muscular activity suggests that such a preslaughter treatment can have an effect on post-mortem muscle integrity. Keywords: Proteome; muscle; trout; preslaughter procedure |
| doi_str_mv | 10.1021/jf0528759 |
| format | Article |
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Muscle was sampled 45 min and 24 h post-mortem, proteins were separated using two-dimensional electrophoresis, and spots of interest were tentatively identified by MALDI-TOF spectrometry. Twenty-nine and 4 spots were differentially represented between the two groups of fish at 45 min and 24 h post-mortem, respectively. Spots that could be identified corresponded mainly to proteins involved in energy-producing pathways (triosephosphate isomerase, enolase, pyruvate dehydrogenase) or to structural proteins (desmin, cap-Z, myosin heavy chain fragment). Persistent under-representation of desmin, a key cytoskeletal protein, in fish submitted to intense muscular activity suggests that such a preslaughter treatment can have an effect on post-mortem muscle integrity. Keywords: Proteome; muscle; trout; preslaughter procedure</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf0528759</identifier><identifier>PMID: 16608221</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Animals ; Biological and medical sciences ; CapZ Actin Capping Protein - analysis ; Desmin - analysis ; Electrophoresis, Gel, Two-Dimensional ; Fish and seafood industries ; Food engineering ; Food Handling - methods ; Food industries ; Fundamental and applied biological sciences. Psychology ; Life Sciences ; Muscle Proteins - analysis ; Myosin Heavy Chains - analysis ; Oncorhynchus mykiss ; Postmortem Changes ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Time Factors</subject><ispartof>Journal of agricultural and food chemistry, 2006-04, Vol.54 (8), p.2997-3001</ispartof><rights>Copyright © 2006 American Chemical Society</rights><rights>2006 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a512t-2fea131099e19de7bb310a55280cb3e40b51d3ee2bf3af5aadf45c5e8936556b3</citedby><cites>FETCH-LOGICAL-a512t-2fea131099e19de7bb310a55280cb3e40b51d3ee2bf3af5aadf45c5e8936556b3</cites><orcidid>0000-0002-5573-8411 ; 0000-0002-3589-3641 ; 0000-0003-0357-9807</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf0528759$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf0528759$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,776,780,881,2751,27054,27902,27903,56715,56765</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17709005$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16608221$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02655423$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Morzel, Martine</creatorcontrib><creatorcontrib>Chambon, Christophe</creatorcontrib><creatorcontrib>Lefèvre, Florence</creatorcontrib><creatorcontrib>Paboeuf, Gilles</creatorcontrib><creatorcontrib>Laville, Elisabeth</creatorcontrib><title>Modifications of Trout (Oncorhynchus mykiss) Muscle Proteins by Preslaughter Activity</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>The effect of two different preslaughter procedures (limited or 15-min intense muscular activity) on muscle trout proteins was investigated. Muscle was sampled 45 min and 24 h post-mortem, proteins were separated using two-dimensional electrophoresis, and spots of interest were tentatively identified by MALDI-TOF spectrometry. Twenty-nine and 4 spots were differentially represented between the two groups of fish at 45 min and 24 h post-mortem, respectively. Spots that could be identified corresponded mainly to proteins involved in energy-producing pathways (triosephosphate isomerase, enolase, pyruvate dehydrogenase) or to structural proteins (desmin, cap-Z, myosin heavy chain fragment). Persistent under-representation of desmin, a key cytoskeletal protein, in fish submitted to intense muscular activity suggests that such a preslaughter treatment can have an effect on post-mortem muscle integrity. Keywords: Proteome; muscle; trout; preslaughter procedure</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>CapZ Actin Capping Protein - analysis</subject><subject>Desmin - analysis</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Fish and seafood industries</subject><subject>Food engineering</subject><subject>Food Handling - methods</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Life Sciences</subject><subject>Muscle Proteins - analysis</subject><subject>Myosin Heavy Chains - analysis</subject><subject>Oncorhynchus mykiss</subject><subject>Postmortem Changes</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Time Factors</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c9v0zAUB3ALgVgZHPgHUC6g7ZDxbNd2cqy2QUGdNqBD3CzHsam7NB62M5H_Hk-t2gvSTv7xPnr20xehtxjOMBD8cW2BkUqw-hmaYEagZBhXz9EEcrGsGMdH6FWMawComICX6AhzDhUheIJur3zrrNMqOd_HwttiGfyQipPrXvuwGnu9GmKxGe9cjKfF1RB1Z4qb4JNxmTdj3pvYqeH3KplQzHRyDy6Nr9ELq7po3uzWY3T76XJ5Pi8X15-_nM8WpWKYpJJYozDFUNcG160RTZMPiuVZQDfUTKFhuKXGkMZSZZlSrZ0yzUxVU84Yb-gxOt32XalO3ge3UWGUXjk5ny3k4x2QDKeEPuBsP2ztffB_BhOT3LioTdep3vghSi4qniV_EuKaiZoTenhdBx9jMHb_BQzyMRi5Dybbd7umQ7Mx7UHuksjg_Q6oqFVng-q1iwcnBNQALLty61xM5u--rsJdnoAKJpc3P-TF_Lv49fPbhfx66Kt0lGs_hD4H8p8P_gMb3q-D</recordid><startdate>20060419</startdate><enddate>20060419</enddate><creator>Morzel, Martine</creator><creator>Chambon, Christophe</creator><creator>Lefèvre, Florence</creator><creator>Paboeuf, Gilles</creator><creator>Laville, Elisabeth</creator><general>American Chemical Society</general><scope>BSCLL</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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-5573-8411</orcidid><orcidid>https://orcid.org/0000-0002-3589-3641</orcidid><orcidid>https://orcid.org/0000-0003-0357-9807</orcidid></search><sort><creationdate>20060419</creationdate><title>Modifications of Trout (Oncorhynchus mykiss) Muscle Proteins by Preslaughter Activity</title><author>Morzel, Martine ; Chambon, Christophe ; Lefèvre, Florence ; Paboeuf, Gilles ; Laville, Elisabeth</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a512t-2fea131099e19de7bb310a55280cb3e40b51d3ee2bf3af5aadf45c5e8936556b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>CapZ Actin Capping Protein - analysis</topic><topic>Desmin - analysis</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Fish and seafood industries</topic><topic>Food engineering</topic><topic>Food Handling - methods</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Life Sciences</topic><topic>Muscle Proteins - analysis</topic><topic>Myosin Heavy Chains - analysis</topic><topic>Oncorhynchus mykiss</topic><topic>Postmortem Changes</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Morzel, Martine</creatorcontrib><creatorcontrib>Chambon, Christophe</creatorcontrib><creatorcontrib>Lefèvre, Florence</creatorcontrib><creatorcontrib>Paboeuf, Gilles</creatorcontrib><creatorcontrib>Laville, Elisabeth</creatorcontrib><collection>Istex</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>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Morzel, Martine</au><au>Chambon, Christophe</au><au>Lefèvre, Florence</au><au>Paboeuf, Gilles</au><au>Laville, Elisabeth</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Modifications of Trout (Oncorhynchus mykiss) Muscle Proteins by Preslaughter Activity</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2006-04-19</date><risdate>2006</risdate><volume>54</volume><issue>8</issue><spage>2997</spage><epage>3001</epage><pages>2997-3001</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>The effect of two different preslaughter procedures (limited or 15-min intense muscular activity) on muscle trout proteins was investigated. Muscle was sampled 45 min and 24 h post-mortem, proteins were separated using two-dimensional electrophoresis, and spots of interest were tentatively identified by MALDI-TOF spectrometry. Twenty-nine and 4 spots were differentially represented between the two groups of fish at 45 min and 24 h post-mortem, respectively. Spots that could be identified corresponded mainly to proteins involved in energy-producing pathways (triosephosphate isomerase, enolase, pyruvate dehydrogenase) or to structural proteins (desmin, cap-Z, myosin heavy chain fragment). Persistent under-representation of desmin, a key cytoskeletal protein, in fish submitted to intense muscular activity suggests that such a preslaughter treatment can have an effect on post-mortem muscle integrity. Keywords: Proteome; muscle; trout; preslaughter procedure</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>16608221</pmid><doi>10.1021/jf0528759</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0002-5573-8411</orcidid><orcidid>https://orcid.org/0000-0002-3589-3641</orcidid><orcidid>https://orcid.org/0000-0003-0357-9807</orcidid></addata></record> |
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| ispartof | Journal of agricultural and food chemistry, 2006-04, Vol.54 (8), p.2997-3001 |
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| source | ACS Publications; MEDLINE |
| subjects | Animals Biological and medical sciences CapZ Actin Capping Protein - analysis Desmin - analysis Electrophoresis, Gel, Two-Dimensional Fish and seafood industries Food engineering Food Handling - methods Food industries Fundamental and applied biological sciences. Psychology Life Sciences Muscle Proteins - analysis Myosin Heavy Chains - analysis Oncorhynchus mykiss Postmortem Changes Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Time Factors |
| title | Modifications of Trout (Oncorhynchus mykiss) Muscle Proteins by Preslaughter Activity |
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