Interaction of paratropomyosin with beta-connectin and its 400-kiloDalton fragment from chicken skeletal muscle as influenced by the calcium ion concentration
The binding of paratropomyosin to β-connectin, which has been suggested to interact at the A-I junction of a sarcomere, was confirmed by measuring the changes in turbidity of a mixture with changing NaCl concentration, pH and free calcium ions, and by morphological observation and a coprecipitation...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1999-08, Vol.63 (8), p.1425-1432 |
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| container_title | Bioscience, biotechnology, and biochemistry |
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| creator | Fei, S. (Kobe Univ. (Japan)) Yamanoue, M Okayama, T |
| description | The binding of paratropomyosin to β-connectin, which has been suggested to interact at the A-I junction of a sarcomere, was confirmed by measuring the changes in turbidity of a mixture with changing NaCl concentration, pH and free calcium ions, and by morphological observation and a coprecipitation assay of the aggregates formed in the mixture. Paratropomyosin also bound to the 400-kDa fragment which is the N-terminal portion of β-connectin and contains the A-I junction region. Moreover, the interaction of paratropomyosin with the 400-kDa fragment was enhanced by a calcium ion concentration from 10
-7
M to 10
-5
M and markedly suppressed above 10
-4
M calcium ions. We conclude that paratropomyosin probably binds to the 400-kDa fragment of β-connectin in the A-I junction region in living and pre-rigor skeletal muscle. In postmortem skeletal muscle paratropomyosin may be released from the 400-kDa portion of the connectin filament by increased calcium ion concentration and translocated on to thin filaments to induce meat tenderization. |
| doi_str_mv | 10.1271/bbb.63.1425 |
| format | Article |
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-7
M to 10
-5
M and markedly suppressed above 10
-4
M calcium ions. We conclude that paratropomyosin probably binds to the 400-kDa fragment of β-connectin in the A-I junction region in living and pre-rigor skeletal muscle. In postmortem skeletal muscle paratropomyosin may be released from the 400-kDa portion of the connectin filament by increased calcium ion concentration and translocated on to thin filaments to induce meat tenderization.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.63.1425</identifier><identifier>PMID: 10501002</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>400-kDa fragment ; Animals ; Biological and medical sciences ; CALCIO ; CALCIUM ; Calcium - analysis ; CHICKENS ; Connectin ; Food industries ; Fundamental and applied biological sciences. Psychology ; Meat and meat product industries ; meat tenderization ; Membranes, Artificial ; MIOSINA ; Molecular Weight ; MUSCLE ; Muscle Proteins - chemistry ; Muscle, Skeletal - chemistry ; MUSCLES ; MUSCULOS ; MYOSIN ; MYOSINE ; Nephelometry and Turbidimetry ; paratropomyosin ; Peptide Fragments - chemistry ; POLLO ; postmortem ageing ; POULET ; Protein Binding ; Protein Kinases - chemistry ; Tropomyosin - chemistry ; β-connectin</subject><ispartof>Bioscience, biotechnology, and biochemistry, 1999-08, Vol.63 (8), p.1425-1432</ispartof><rights>1999 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 1999</rights><rights>1999 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c486t-ea1b3650739fce6569a991c32ca47cd60e559b29417bde35938a151751ed5dbc3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1988460$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10501002$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fei, S. (Kobe Univ. (Japan))</creatorcontrib><creatorcontrib>Yamanoue, M</creatorcontrib><creatorcontrib>Okayama, T</creatorcontrib><title>Interaction of paratropomyosin with beta-connectin and its 400-kiloDalton fragment from chicken skeletal muscle as influenced by the calcium ion concentration</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>The binding of paratropomyosin to β-connectin, which has been suggested to interact at the A-I junction of a sarcomere, was confirmed by measuring the changes in turbidity of a mixture with changing NaCl concentration, pH and free calcium ions, and by morphological observation and a coprecipitation assay of the aggregates formed in the mixture. Paratropomyosin also bound to the 400-kDa fragment which is the N-terminal portion of β-connectin and contains the A-I junction region. Moreover, the interaction of paratropomyosin with the 400-kDa fragment was enhanced by a calcium ion concentration from 10
-7
M to 10
-5
M and markedly suppressed above 10
-4
M calcium ions. We conclude that paratropomyosin probably binds to the 400-kDa fragment of β-connectin in the A-I junction region in living and pre-rigor skeletal muscle. In postmortem skeletal muscle paratropomyosin may be released from the 400-kDa portion of the connectin filament by increased calcium ion concentration and translocated on to thin filaments to induce meat tenderization.</description><subject>400-kDa fragment</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>CALCIO</subject><subject>CALCIUM</subject><subject>Calcium - analysis</subject><subject>CHICKENS</subject><subject>Connectin</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Meat and meat product industries</subject><subject>meat tenderization</subject><subject>Membranes, Artificial</subject><subject>MIOSINA</subject><subject>Molecular Weight</subject><subject>MUSCLE</subject><subject>Muscle Proteins - chemistry</subject><subject>Muscle, Skeletal - chemistry</subject><subject>MUSCLES</subject><subject>MUSCULOS</subject><subject>MYOSIN</subject><subject>MYOSINE</subject><subject>Nephelometry and Turbidimetry</subject><subject>paratropomyosin</subject><subject>Peptide Fragments - chemistry</subject><subject>POLLO</subject><subject>postmortem ageing</subject><subject>POULET</subject><subject>Protein Binding</subject><subject>Protein Kinases - chemistry</subject><subject>Tropomyosin - chemistry</subject><subject>β-connectin</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkTuP1DAUhSMEYoeFihrkAtGgDHb8SFyi5bVoJSigjm6cmx0zjj3YjlbzZ_iteMggKHDjh75zfHRuVT1ldMualr0ehmGr-JaJRt6rNoyLtlZatPerDdVM1Z2Q7KJ6lNJ3SsuDZA-rC0YlZZQ2m-rntc8YwWQbPAkTOUCEHMMhzMeQrCd3Nu_IgBlqE7zHwnkCfiQ2JyIorffWhbfgclFPEW5n9LkcwkzMzpo9epL26IrckXlJxiGBRKyf3ILe4EiGI8k7JAacsctMTiHKP6a4lBjl9rh6MIFL-OS8X1bf3r_7evWxvvn84frqzU1tRKdyjcAGriRtuZ4MKqk0aM0MbwyI1oyKopR6aLRg7TAil5p3UJpoJcNRjoPhl9XL1fcQw48FU-5nmww6Bx7DkvqWth0VqingqxU0MaQUceoP0c4Qjz2j_WkcfRlHr3h_Gkehn59tl2HG8R927b8AL84ApFJCqdAbm_5yuuuEogVTK1aqC3GGuxDd2Gc4uhD_aPj_AzxbhROEHm5j4T59aejvpXXLfwHhe7Cy</recordid><startdate>19990801</startdate><enddate>19990801</enddate><creator>Fei, S. (Kobe Univ. (Japan))</creator><creator>Yamanoue, M</creator><creator>Okayama, T</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</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>19990801</creationdate><title>Interaction of paratropomyosin with beta-connectin and its 400-kiloDalton fragment from chicken skeletal muscle as influenced by the calcium ion concentration</title><author>Fei, S. (Kobe Univ. (Japan)) ; Yamanoue, M ; Okayama, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c486t-ea1b3650739fce6569a991c32ca47cd60e559b29417bde35938a151751ed5dbc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>400-kDa fragment</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>CALCIO</topic><topic>CALCIUM</topic><topic>Calcium - analysis</topic><topic>CHICKENS</topic><topic>Connectin</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Meat and meat product industries</topic><topic>meat tenderization</topic><topic>Membranes, Artificial</topic><topic>MIOSINA</topic><topic>Molecular Weight</topic><topic>MUSCLE</topic><topic>Muscle Proteins - chemistry</topic><topic>Muscle, Skeletal - chemistry</topic><topic>MUSCLES</topic><topic>MUSCULOS</topic><topic>MYOSIN</topic><topic>MYOSINE</topic><topic>Nephelometry and Turbidimetry</topic><topic>paratropomyosin</topic><topic>Peptide Fragments - chemistry</topic><topic>POLLO</topic><topic>postmortem ageing</topic><topic>POULET</topic><topic>Protein Binding</topic><topic>Protein Kinases - chemistry</topic><topic>Tropomyosin - chemistry</topic><topic>β-connectin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fei, S. (Kobe Univ. (Japan))</creatorcontrib><creatorcontrib>Yamanoue, M</creatorcontrib><creatorcontrib>Okayama, T</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>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fei, S. (Kobe Univ. (Japan))</au><au>Yamanoue, M</au><au>Okayama, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of paratropomyosin with beta-connectin and its 400-kiloDalton fragment from chicken skeletal muscle as influenced by the calcium ion concentration</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>1999-08-01</date><risdate>1999</risdate><volume>63</volume><issue>8</issue><spage>1425</spage><epage>1432</epage><pages>1425-1432</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>The binding of paratropomyosin to β-connectin, which has been suggested to interact at the A-I junction of a sarcomere, was confirmed by measuring the changes in turbidity of a mixture with changing NaCl concentration, pH and free calcium ions, and by morphological observation and a coprecipitation assay of the aggregates formed in the mixture. Paratropomyosin also bound to the 400-kDa fragment which is the N-terminal portion of β-connectin and contains the A-I junction region. Moreover, the interaction of paratropomyosin with the 400-kDa fragment was enhanced by a calcium ion concentration from 10
-7
M to 10
-5
M and markedly suppressed above 10
-4
M calcium ions. We conclude that paratropomyosin probably binds to the 400-kDa fragment of β-connectin in the A-I junction region in living and pre-rigor skeletal muscle. In postmortem skeletal muscle paratropomyosin may be released from the 400-kDa portion of the connectin filament by increased calcium ion concentration and translocated on to thin filaments to induce meat tenderization.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>10501002</pmid><doi>10.1271/bbb.63.1425</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Bioscience, biotechnology, and biochemistry, 1999-08, Vol.63 (8), p.1425-1432 |
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| language | eng |
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| source | J-STAGE Free; MEDLINE; Oxford University Press Journals All Titles (1996-Current); Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | 400-kDa fragment Animals Biological and medical sciences CALCIO CALCIUM Calcium - analysis CHICKENS Connectin Food industries Fundamental and applied biological sciences. Psychology Meat and meat product industries meat tenderization Membranes, Artificial MIOSINA Molecular Weight MUSCLE Muscle Proteins - chemistry Muscle, Skeletal - chemistry MUSCLES MUSCULOS MYOSIN MYOSINE Nephelometry and Turbidimetry paratropomyosin Peptide Fragments - chemistry POLLO postmortem ageing POULET Protein Binding Protein Kinases - chemistry Tropomyosin - chemistry β-connectin |
| title | Interaction of paratropomyosin with beta-connectin and its 400-kiloDalton fragment from chicken skeletal muscle as influenced by the calcium ion concentration |
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