Characterization of the C-protein from posterior latissimus dorsi muscle of the adult chicken: heterogeneity within a single sarcomere
Specific isoforms of myofibrillar proteins are expressed in different muscles and in various fiber types within a single muscle. We have isolated and characterized monoclonal antibodies against C-proteins from slow tonic (anterior latissimus dorsi, ALD) and fast twich (pectoralis major) muscles of t...
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| Veröffentlicht in: | The Journal of cell biology 1983-01, Vol.96 (1), p.297-300 |
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| container_title | The Journal of cell biology |
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| creator | Reinach, F.C Masaki, T Fischman, D.A |
| description | Specific isoforms of myofibrillar proteins are expressed in different muscles and in various fiber types within a single muscle. We have isolated and characterized monoclonal antibodies against C-proteins from slow tonic (anterior latissimus dorsi, ALD) and fast twich (pectoralis major) muscles of the chicken. Although the antibody against "fast" C-protein (MF-1) did not bind to the "slow" isoform and the antibody to the "slow" C-protein (ALD-66) did not bind to the "fast" isoform, we observed that both antibodies bound C-protein from the posterior latissimus dorsi (PLD) muscle. Here we demonstrate that in the PLD muscle the binding sites of these two antibodies reside in two different C-protein isoforms which have different molecular weights and can be separated by hydroxylapatite column chromatography. Since we have shown previously that both these antibodies stain all myofibers and myofibrils derived from PLD muscle, we conclude that all myofibers in this muscle contain both isoforms within all sarcomeres. |
| doi_str_mv | 10.1083/jcb.96.1.297 |
| format | Article |
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We have isolated and characterized monoclonal antibodies against C-proteins from slow tonic (anterior latissimus dorsi, ALD) and fast twich (pectoralis major) muscles of the chicken. Although the antibody against "fast" C-protein (MF-1) did not bind to the "slow" isoform and the antibody to the "slow" C-protein (ALD-66) did not bind to the "fast" isoform, we observed that both antibodies bound C-protein from the posterior latissimus dorsi (PLD) muscle. Here we demonstrate that in the PLD muscle the binding sites of these two antibodies reside in two different C-protein isoforms which have different molecular weights and can be separated by hydroxylapatite column chromatography. Since we have shown previously that both these antibodies stain all myofibers and myofibrils derived from PLD muscle, we conclude that all myofibers in this muscle contain both isoforms within all sarcomeres.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.96.1.297</identifier><identifier>PMID: 6687470</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Animals ; Antibodies ; Antibodies, Monoclonal ; Antigens ; Carrier Proteins ; Chickens ; Chromatography ; Gels ; Hydroxyapatites ; Molecular Weight ; Muscle Proteins - analysis ; Muscle Proteins - immunology ; Muscle Proteins - isolation & purification ; Myofibrils ; Myofibrils - analysis ; Protein isoforms ; Radioimmunoassay ; Rapid Communications ; Skeletal muscle ; Solid phases</subject><ispartof>The Journal of cell biology, 1983-01, Vol.96 (1), p.297-300</ispartof><rights>Copyright 1983 The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c419t-c82ba41bf505087a695fc5049820aad4590ff6b85842042052d1fbe9f1bd89f73</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6687470$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reinach, F.C</creatorcontrib><creatorcontrib>Masaki, T</creatorcontrib><creatorcontrib>Fischman, D.A</creatorcontrib><title>Characterization of the C-protein from posterior latissimus dorsi muscle of the adult chicken: heterogeneity within a single sarcomere</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Specific isoforms of myofibrillar proteins are expressed in different muscles and in various fiber types within a single muscle. We have isolated and characterized monoclonal antibodies against C-proteins from slow tonic (anterior latissimus dorsi, ALD) and fast twich (pectoralis major) muscles of the chicken. Although the antibody against "fast" C-protein (MF-1) did not bind to the "slow" isoform and the antibody to the "slow" C-protein (ALD-66) did not bind to the "fast" isoform, we observed that both antibodies bound C-protein from the posterior latissimus dorsi (PLD) muscle. Here we demonstrate that in the PLD muscle the binding sites of these two antibodies reside in two different C-protein isoforms which have different molecular weights and can be separated by hydroxylapatite column chromatography. Since we have shown previously that both these antibodies stain all myofibers and myofibrils derived from PLD muscle, we conclude that all myofibers in this muscle contain both isoforms within all sarcomeres.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, Monoclonal</subject><subject>Antigens</subject><subject>Carrier Proteins</subject><subject>Chickens</subject><subject>Chromatography</subject><subject>Gels</subject><subject>Hydroxyapatites</subject><subject>Molecular Weight</subject><subject>Muscle Proteins - analysis</subject><subject>Muscle Proteins - immunology</subject><subject>Muscle Proteins - isolation & purification</subject><subject>Myofibrils</subject><subject>Myofibrils - analysis</subject><subject>Protein isoforms</subject><subject>Radioimmunoassay</subject><subject>Rapid Communications</subject><subject>Skeletal muscle</subject><subject>Solid phases</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkcFvFCEYxYnR1LV682Q04dSTs34wMAMeTMxGrUmTHrRnwjCwwzozrMBo2j_Av1ua3VabQCB5v_c-wkPoJYE1AVG_25luLZs1WVPZPkIrwhlUgjB4jFYAlFSSU_4UPUtpBwCsZfUJOmka0bIWVujPZtBRm2yjv9HZhxkHh_Ng8abax5Ctn7GLYcL7kG6ZEPFYsJT8tCTch5g8Ljcz2juf7pcxYzN488PO7_Fgiy1s7Wx9vsa_fR5KosbJz9viSTqaMNlon6MnTo_Jvjiep-jq86fvm_Pq4vLL183Hi8owInNlBO00I53jwEG0upHcGQ5MCgpa94xLcK7pBBeMQlmc9sR1VjrS9UK6tj5FHw65-6WbbG_snKMe1T76ScdrFbRXD5XZD2obfilKCKVNXQLOjgEx_Fxsymryydhx1LMNS1IC6rZsKODbA2hiSCladz-EgLrtTZXelGwUUaW3gr_5_2H38LGoor8-6LuUQ_yX1RAoX1HkVwfZ6aD0Nvqkrr4JygVnbf0X-3epUw</recordid><startdate>198301</startdate><enddate>198301</enddate><creator>Reinach, F.C</creator><creator>Masaki, T</creator><creator>Fischman, D.A</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>FBQ</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><scope>5PM</scope></search><sort><creationdate>198301</creationdate><title>Characterization of the C-protein from posterior latissimus dorsi muscle of the adult chicken: heterogeneity within a single sarcomere</title><author>Reinach, F.C ; Masaki, T ; Fischman, D.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c419t-c82ba41bf505087a695fc5049820aad4590ff6b85842042052d1fbe9f1bd89f73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies, Monoclonal</topic><topic>Antigens</topic><topic>Carrier Proteins</topic><topic>Chickens</topic><topic>Chromatography</topic><topic>Gels</topic><topic>Hydroxyapatites</topic><topic>Molecular Weight</topic><topic>Muscle Proteins - analysis</topic><topic>Muscle Proteins - immunology</topic><topic>Muscle Proteins - isolation & purification</topic><topic>Myofibrils</topic><topic>Myofibrils - analysis</topic><topic>Protein isoforms</topic><topic>Radioimmunoassay</topic><topic>Rapid Communications</topic><topic>Skeletal muscle</topic><topic>Solid phases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reinach, F.C</creatorcontrib><creatorcontrib>Masaki, T</creatorcontrib><creatorcontrib>Fischman, D.A</creatorcontrib><collection>AGRIS</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reinach, F.C</au><au>Masaki, T</au><au>Fischman, D.A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the C-protein from posterior latissimus dorsi muscle of the adult chicken: heterogeneity within a single sarcomere</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1983-01</date><risdate>1983</risdate><volume>96</volume><issue>1</issue><spage>297</spage><epage>300</epage><pages>297-300</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><abstract>Specific isoforms of myofibrillar proteins are expressed in different muscles and in various fiber types within a single muscle. We have isolated and characterized monoclonal antibodies against C-proteins from slow tonic (anterior latissimus dorsi, ALD) and fast twich (pectoralis major) muscles of the chicken. Although the antibody against "fast" C-protein (MF-1) did not bind to the "slow" isoform and the antibody to the "slow" C-protein (ALD-66) did not bind to the "fast" isoform, we observed that both antibodies bound C-protein from the posterior latissimus dorsi (PLD) muscle. Here we demonstrate that in the PLD muscle the binding sites of these two antibodies reside in two different C-protein isoforms which have different molecular weights and can be separated by hydroxylapatite column chromatography. Since we have shown previously that both these antibodies stain all myofibers and myofibrils derived from PLD muscle, we conclude that all myofibers in this muscle contain both isoforms within all sarcomeres.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>6687470</pmid><doi>10.1083/jcb.96.1.297</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9525 |
| ispartof | The Journal of cell biology, 1983-01, Vol.96 (1), p.297-300 |
| issn | 0021-9525 1540-8140 |
| language | eng |
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| source | MEDLINE; Free E-Journal (出版社公開部分のみ）; Alma/SFX Local Collection |
| subjects | Animals Antibodies Antibodies, Monoclonal Antigens Carrier Proteins Chickens Chromatography Gels Hydroxyapatites Molecular Weight Muscle Proteins - analysis Muscle Proteins - immunology Muscle Proteins - isolation & purification Myofibrils Myofibrils - analysis Protein isoforms Radioimmunoassay Rapid Communications Skeletal muscle Solid phases |
| title | Characterization of the C-protein from posterior latissimus dorsi muscle of the adult chicken: heterogeneity within a single sarcomere |
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