Meat tenderness: distribution of molecular species of collagen in bovine muscle
The collagen of bovine striated muscle has been shown to be comprised of three genetically distinct types of collagen, the proportions of which vary from the tendon to the endomysium. Despite the variation in genetic type all three collagens are stabilised by lysine‐derived cross‐links. It is propos...
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| Veröffentlicht in: | Journal of the science of food and agriculture 1977-06, Vol.28 (6), p.565-570 |
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| container_title | Journal of the science of food and agriculture |
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| creator | Bailey, A.J Sims, T.J |
| description | The collagen of bovine striated muscle has been shown to be comprised of three genetically distinct types of collagen, the proportions of which vary from the tendon to the endomysium. Despite the variation in genetic type all three collagens are stabilised by lysine‐derived cross‐links. It is proposed that the change in the tenderness of meat at temperatures above 65°C is caused by the tension generated during thermal contraction of all three types of collagen and that the extent is determined by the thermal stability of the intermolecular cross‐links. The relative contributions of each type of collagen remain to be elucidated. |
| doi_str_mv | 10.1002/jsfa.2740280615 |
| format | Article |
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Despite the variation in genetic type all three collagens are stabilised by lysine‐derived cross‐links. It is proposed that the change in the tenderness of meat at temperatures above 65°C is caused by the tension generated during thermal contraction of all three types of collagen and that the extent is determined by the thermal stability of the intermolecular cross‐links. The relative contributions of each type of collagen remain to be elucidated.</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.2740280615</identifier><identifier>PMID: 881790</identifier><language>eng</language><publisher>London: John Wiley & Sons, Ltd</publisher><subject>animal products ; Animals ; Cattle ; Chemical Phenomena ; Chemistry ; Collagen ; Connective Tissue ; Drug Stability ; Genetics ; Hot Temperature ; Male ; Meat - standards ; Muscles ; Tendons</subject><ispartof>Journal of the science of food and agriculture, 1977-06, Vol.28 (6), p.565-570</ispartof><rights>Copyright © 1977 John Wiley & Sons, Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4995-90aabbda9fb46a839580e33e92c1f1402c25b6fb4548379fa241208ae26975f3</citedby><cites>FETCH-LOGICAL-c4995-90aabbda9fb46a839580e33e92c1f1402c25b6fb4548379fa241208ae26975f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjsfa.2740280615$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.2740280615$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27846,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/881790$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bailey, A.J</creatorcontrib><creatorcontrib>Sims, T.J</creatorcontrib><title>Meat tenderness: distribution of molecular species of collagen in bovine muscle</title><title>Journal of the science of food and agriculture</title><addtitle>J. Sci. Food Agric</addtitle><description>The collagen of bovine striated muscle has been shown to be comprised of three genetically distinct types of collagen, the proportions of which vary from the tendon to the endomysium. Despite the variation in genetic type all three collagens are stabilised by lysine‐derived cross‐links. It is proposed that the change in the tenderness of meat at temperatures above 65°C is caused by the tension generated during thermal contraction of all three types of collagen and that the extent is determined by the thermal stability of the intermolecular cross‐links. The relative contributions of each type of collagen remain to be elucidated.</description><subject>animal products</subject><subject>Animals</subject><subject>Cattle</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Collagen</subject><subject>Connective Tissue</subject><subject>Drug Stability</subject><subject>Genetics</subject><subject>Hot Temperature</subject><subject>Male</subject><subject>Meat - standards</subject><subject>Muscles</subject><subject>Tendons</subject><issn>0022-5142</issn><issn>1097-0010</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1977</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>K30</sourceid><recordid>eNqFkc1v1DAQxS3E11I4c0EiEhK3tGM7ie1yKhX9QC0V6iKOluMdV16SeLGTlv73eJWqFVx6suT3e08zbwh5S2GXArC9dXJml4kKmISG1k_IgoISJQCFp2SRCVbWtGIvyauU1gCgVNO8IM-lpELBglycoxmLEYcVxgFT2i9WPo3Rt9Pow1AEV_ShQzt1JhZpg9Zj2n7a0HXmCofCD0Ubrv2ART8l2-Fr8syZLuGbu3eHLI--LA9PyrOL49PDg7PSVkrVpQJj2nZllGurxkiuagnIOSpmqaN5GcvqtsliXUkulDOsogykQdYoUTu-Qz7OsZsYfk-YRt37ZDEPNWCYkpYVUEErlcEP_4HrMMUhj6YpB04pVw1kam-mbAwpRXR6E31v4q2moLc1623N-qHm7Hh3lzu1Pa7u-bnXLH-a5Rvf4e1jafrr5dHBP-Hl7M6nwD_3bhN_6UZwUeuf3461-K5OpOCf9TLz72femaDNVfRJ_7hkkBdkSuQagP8FwMahDQ</recordid><startdate>197706</startdate><enddate>197706</enddate><creator>Bailey, A.J</creator><creator>Sims, T.J</creator><general>John Wiley & Sons, Ltd</general><general>Published for the Society of Chemical Industry by Elsevier Applied Science</general><scope>FBQ</scope><scope>BSCLL</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>HJHVS</scope><scope>IZSXY</scope><scope>K30</scope><scope>PAAUG</scope><scope>PAWHS</scope><scope>PAWZZ</scope><scope>PAXOH</scope><scope>PBHAV</scope><scope>PBQSW</scope><scope>PBYQZ</scope><scope>PCIWU</scope><scope>PCMID</scope><scope>PCZJX</scope><scope>PDGRG</scope><scope>PDWWI</scope><scope>PETMR</scope><scope>PFVGT</scope><scope>PGXDX</scope><scope>PIHIL</scope><scope>PISVA</scope><scope>PJCTQ</scope><scope>PJTMS</scope><scope>PLCHJ</scope><scope>PMHAD</scope><scope>PNQDJ</scope><scope>POUND</scope><scope>PPLAD</scope><scope>PQAPC</scope><scope>PQCAN</scope><scope>PQCMW</scope><scope>PQEME</scope><scope>PQHKH</scope><scope>PQMID</scope><scope>PQNCT</scope><scope>PQNET</scope><scope>PQSCT</scope><scope>PQSET</scope><scope>PSVJG</scope><scope>PVMQY</scope><scope>PZGFC</scope><scope>7X8</scope></search><sort><creationdate>197706</creationdate><title>Meat tenderness: distribution of molecular species of collagen in bovine muscle</title><author>Bailey, A.J ; Sims, T.J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4995-90aabbda9fb46a839580e33e92c1f1402c25b6fb4548379fa241208ae26975f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1977</creationdate><topic>animal products</topic><topic>Animals</topic><topic>Cattle</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Collagen</topic><topic>Connective Tissue</topic><topic>Drug Stability</topic><topic>Genetics</topic><topic>Hot Temperature</topic><topic>Male</topic><topic>Meat - standards</topic><topic>Muscles</topic><topic>Tendons</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bailey, A.J</creatorcontrib><creatorcontrib>Sims, T.J</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Periodicals Index Online Segment 19</collection><collection>Periodicals Index Online Segment 30</collection><collection>Periodicals Index Online</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - West</collection><collection>Primary Sources Access (Plan D) - International</collection><collection>Primary Sources Access & Build (Plan A) - MEA</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - Midwest</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - Northeast</collection><collection>Primary Sources Access (Plan D) - Southeast</collection><collection>Primary Sources Access (Plan D) - North Central</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - Southeast</collection><collection>Primary Sources Access (Plan D) - South Central</collection><collection>Primary Sources Access & Build (Plan A) - UK / I</collection><collection>Primary Sources Access (Plan D) - Canada</collection><collection>Primary Sources Access (Plan D) - EMEALA</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - North Central</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - South Central</collection><collection>Primary Sources Access & Build (Plan A) - International</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - International</collection><collection>Primary Sources Access (Plan D) - West</collection><collection>Periodicals Index Online Segments 1-50</collection><collection>Primary Sources Access (Plan D) - APAC</collection><collection>Primary Sources Access (Plan D) - Midwest</collection><collection>Primary Sources Access (Plan D) - MEA</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - Canada</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - UK / I</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - EMEALA</collection><collection>Primary Sources Access & Build (Plan A) - APAC</collection><collection>Primary Sources Access & Build (Plan A) - Canada</collection><collection>Primary Sources Access & Build (Plan A) - West</collection><collection>Primary Sources Access & Build (Plan A) - EMEALA</collection><collection>Primary Sources Access (Plan D) - Northeast</collection><collection>Primary Sources Access & Build (Plan A) - Midwest</collection><collection>Primary Sources Access & Build (Plan A) - North Central</collection><collection>Primary Sources Access & Build (Plan A) - Northeast</collection><collection>Primary Sources Access & Build (Plan A) - South Central</collection><collection>Primary Sources Access & Build (Plan A) - Southeast</collection><collection>Primary Sources Access (Plan D) - UK / I</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - APAC</collection><collection>Primary Sources Access—Foundation Edition (Plan E) - MEA</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the science of food and agriculture</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bailey, A.J</au><au>Sims, T.J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Meat tenderness: distribution of molecular species of collagen in bovine muscle</atitle><jtitle>Journal of the science of food and agriculture</jtitle><addtitle>J. Sci. Food Agric</addtitle><date>1977-06</date><risdate>1977</risdate><volume>28</volume><issue>6</issue><spage>565</spage><epage>570</epage><pages>565-570</pages><issn>0022-5142</issn><eissn>1097-0010</eissn><abstract>The collagen of bovine striated muscle has been shown to be comprised of three genetically distinct types of collagen, the proportions of which vary from the tendon to the endomysium. Despite the variation in genetic type all three collagens are stabilised by lysine‐derived cross‐links. It is proposed that the change in the tenderness of meat at temperatures above 65°C is caused by the tension generated during thermal contraction of all three types of collagen and that the extent is determined by the thermal stability of the intermolecular cross‐links. The relative contributions of each type of collagen remain to be elucidated.</abstract><cop>London</cop><pub>John Wiley & Sons, Ltd</pub><pmid>881790</pmid><doi>10.1002/jsfa.2740280615</doi><tpages>6</tpages></addata></record> |
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| ispartof | Journal of the science of food and agriculture, 1977-06, Vol.28 (6), p.565-570 |
| issn | 0022-5142 1097-0010 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Periodicals Index Online |
| subjects | animal products Animals Cattle Chemical Phenomena Chemistry Collagen Connective Tissue Drug Stability Genetics Hot Temperature Male Meat - standards Muscles Tendons |
| title | Meat tenderness: distribution of molecular species of collagen in bovine muscle |
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