Immunohistochemical Localization of Contractile Proteins in Limulus Striated Muscle
Limulus paramyosin and myosin were localized in the A bands of glycerinated Limulus striated muscle by the indirect horseradish peroxidase-labeled antibody and direct and indirect fluorescent antibody techniques. Localization of each protein in the A band varied with sarcomere length. Antiparamyosin...
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| Veröffentlicht in: | The Journal of cell biology 1972-10, Vol.55 (1), p.221-235 |
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| container_title | The Journal of cell biology |
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| creator | Rhea J. C. Levine Dewey, Maynard M. de Villafranca, George W. |
| description | Limulus paramyosin and myosin were localized in the A bands of glycerinated Limulus striated muscle by the indirect horseradish peroxidase-labeled antibody and direct and indirect fluorescent antibody techniques. Localization of each protein in the A band varied with sarcomere length. Antiparamyosin was bound at the lateral margins of the A bands in long (∼ 10.0 μ) and intermediate (∼ 7.0 μ) length sarcomeres, and also in a thin line in the central A bands of sarcomeres, 7.0-∼6.0 μ. Antiparamyosin stained the entire A bands of short sarcomeres ( |
| doi_str_mv | 10.1083/jcb.55.1.221 |
| format | Article |
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C. Levine ; Dewey, Maynard M. ; de Villafranca, George W.</creator><creatorcontrib>Rhea J. C. Levine ; Dewey, Maynard M. ; de Villafranca, George W.</creatorcontrib><description>Limulus paramyosin and myosin were localized in the A bands of glycerinated Limulus striated muscle by the indirect horseradish peroxidase-labeled antibody and direct and indirect fluorescent antibody techniques. Localization of each protein in the A band varied with sarcomere length. Antiparamyosin was bound at the lateral margins of the A bands in long (∼ 10.0 μ) and intermediate (∼ 7.0 μ) length sarcomeres, and also in a thin line in the central A bands of sarcomeres, 7.0-∼6.0 μ. Antiparamyosin stained the entire A bands of short sarcomeres (<6.0). Conversely, antimyosin stained the entire A bands of long sarcomeres, showed decreased intensity of central A band staining except for a thin medial line in intermediate length sarcomeres, and was bound only in the lateral A bands of short sarcomeres. These results are consistent with a model in which paramyosin comprises the core of the thick filament and myosin forms a cortex. Differential staining observed using antiparamyosin and antimyosin at various sarcomere lengths and changes in A band lengths reflect the extent of thick-thin filament interaction and conformational change in the thick filament during sarcomeric shortening.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.55.1.221</identifier><identifier>PMID: 4120073</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Actomyosin - analysis ; Animals ; Antibodies ; Antibody Specificity ; Antigen-Antibody Reactions ; Binding Sites, Antibody ; Biological markers ; Brachyura ; Contractile proteins ; Fluorescent Antibody Technique ; Horseradish ; Marine ; Microscopy, Phase-Contrast ; Models, Biological ; Molecules ; Muscle Proteins - analysis ; Muscles ; Muscles - analysis ; Mustard Plant - enzymology ; Myofibrils ; Myosins - analysis ; Peroxidases - pharmacology ; Plants, Medicinal ; Precipitin Tests ; Rabbits - immunology ; Sarcomeres ; Solar fibrils ; Staining and Labeling ; Striated muscle</subject><ispartof>The Journal of cell biology, 1972-10, Vol.55 (1), p.221-235</ispartof><rights>Copyright 1972 The Rockefeller University Press</rights><rights>Copyright © 1972 by The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c431t-e47b4e00d01944be66699e89ba6d59f2cf2f38efb0a5255c14081b272f4505f83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4120073$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rhea J. C. Levine</creatorcontrib><creatorcontrib>Dewey, Maynard M.</creatorcontrib><creatorcontrib>de Villafranca, George W.</creatorcontrib><title>Immunohistochemical Localization of Contractile Proteins in Limulus Striated Muscle</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Limulus paramyosin and myosin were localized in the A bands of glycerinated Limulus striated muscle by the indirect horseradish peroxidase-labeled antibody and direct and indirect fluorescent antibody techniques. Localization of each protein in the A band varied with sarcomere length. Antiparamyosin was bound at the lateral margins of the A bands in long (∼ 10.0 μ) and intermediate (∼ 7.0 μ) length sarcomeres, and also in a thin line in the central A bands of sarcomeres, 7.0-∼6.0 μ. Antiparamyosin stained the entire A bands of short sarcomeres (<6.0). Conversely, antimyosin stained the entire A bands of long sarcomeres, showed decreased intensity of central A band staining except for a thin medial line in intermediate length sarcomeres, and was bound only in the lateral A bands of short sarcomeres. These results are consistent with a model in which paramyosin comprises the core of the thick filament and myosin forms a cortex. Differential staining observed using antiparamyosin and antimyosin at various sarcomere lengths and changes in A band lengths reflect the extent of thick-thin filament interaction and conformational change in the thick filament during sarcomeric shortening.</description><subject>Actomyosin - analysis</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibody Specificity</subject><subject>Antigen-Antibody Reactions</subject><subject>Binding Sites, Antibody</subject><subject>Biological markers</subject><subject>Brachyura</subject><subject>Contractile proteins</subject><subject>Fluorescent Antibody Technique</subject><subject>Horseradish</subject><subject>Marine</subject><subject>Microscopy, Phase-Contrast</subject><subject>Models, Biological</subject><subject>Molecules</subject><subject>Muscle Proteins - analysis</subject><subject>Muscles</subject><subject>Muscles - analysis</subject><subject>Mustard Plant - enzymology</subject><subject>Myofibrils</subject><subject>Myosins - analysis</subject><subject>Peroxidases - pharmacology</subject><subject>Plants, Medicinal</subject><subject>Precipitin Tests</subject><subject>Rabbits - immunology</subject><subject>Sarcomeres</subject><subject>Solar fibrils</subject><subject>Staining and Labeling</subject><subject>Striated muscle</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1972</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFP3DAQha0KRBfaW49FyolTsx07dpxckNCKUqRFVKI9W453zHqVxGA7SOXX49WuoD1xmTm8p6d58xHyhcKcQlN935huLsSczhmjH8iMCg5lQzkckBkAo2UrmPhIjmPcAACXvDoiR5wyAFnNyN31MEyjX7uYvFnj4Izui6XP0z3r5PxYeFss_JiCNsn1WPwKPqEbY-HGYumGqZ9icZeC0wlXxc0UTY-fyKHVfcTP-31C_vy4_L34WS5vr64XF8vS8IqmErnsOAKsgLacd1jXddti03a6XonWMmOZrRq0HejcQJhcqaEdk8xyAcI21Qk53-U-TN2AK4PbK3v1ENygw1_ltVP_K6Nbq3v_pFj-mxTbgLN9QPCPE8akBhcN9r0e0U9RNVQyKip410hly6SsRTZ-2xlN8DEGtK_XUFBbWirTUkIoqjKtbD_9t8GreY8n6193-ibjCW9ZNdSy4dULkmybRQ</recordid><startdate>19721001</startdate><enddate>19721001</enddate><creator>Rhea J. C. Levine</creator><creator>Dewey, Maynard M.</creator><creator>de Villafranca, George W.</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19721001</creationdate><title>Immunohistochemical Localization of Contractile Proteins in Limulus Striated Muscle</title><author>Rhea J. C. Levine ; Dewey, Maynard M. ; de Villafranca, George W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c431t-e47b4e00d01944be66699e89ba6d59f2cf2f38efb0a5255c14081b272f4505f83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1972</creationdate><topic>Actomyosin - analysis</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antibody Specificity</topic><topic>Antigen-Antibody Reactions</topic><topic>Binding Sites, Antibody</topic><topic>Biological markers</topic><topic>Brachyura</topic><topic>Contractile proteins</topic><topic>Fluorescent Antibody Technique</topic><topic>Horseradish</topic><topic>Marine</topic><topic>Microscopy, Phase-Contrast</topic><topic>Models, Biological</topic><topic>Molecules</topic><topic>Muscle Proteins - analysis</topic><topic>Muscles</topic><topic>Muscles - analysis</topic><topic>Mustard Plant - enzymology</topic><topic>Myofibrils</topic><topic>Myosins - analysis</topic><topic>Peroxidases - pharmacology</topic><topic>Plants, Medicinal</topic><topic>Precipitin Tests</topic><topic>Rabbits - immunology</topic><topic>Sarcomeres</topic><topic>Solar fibrils</topic><topic>Staining and Labeling</topic><topic>Striated muscle</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rhea J. C. Levine</creatorcontrib><creatorcontrib>Dewey, Maynard M.</creatorcontrib><creatorcontrib>de Villafranca, George W.</creatorcontrib><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>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>Rhea J. C. Levine</au><au>Dewey, Maynard M.</au><au>de Villafranca, George W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immunohistochemical Localization of Contractile Proteins in Limulus Striated Muscle</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1972-10-01</date><risdate>1972</risdate><volume>55</volume><issue>1</issue><spage>221</spage><epage>235</epage><pages>221-235</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><abstract>Limulus paramyosin and myosin were localized in the A bands of glycerinated Limulus striated muscle by the indirect horseradish peroxidase-labeled antibody and direct and indirect fluorescent antibody techniques. Localization of each protein in the A band varied with sarcomere length. Antiparamyosin was bound at the lateral margins of the A bands in long (∼ 10.0 μ) and intermediate (∼ 7.0 μ) length sarcomeres, and also in a thin line in the central A bands of sarcomeres, 7.0-∼6.0 μ. Antiparamyosin stained the entire A bands of short sarcomeres (<6.0). Conversely, antimyosin stained the entire A bands of long sarcomeres, showed decreased intensity of central A band staining except for a thin medial line in intermediate length sarcomeres, and was bound only in the lateral A bands of short sarcomeres. These results are consistent with a model in which paramyosin comprises the core of the thick filament and myosin forms a cortex. Differential staining observed using antiparamyosin and antimyosin at various sarcomere lengths and changes in A band lengths reflect the extent of thick-thin filament interaction and conformational change in the thick filament during sarcomeric shortening.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>4120073</pmid><doi>10.1083/jcb.55.1.221</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Actomyosin - analysis Animals Antibodies Antibody Specificity Antigen-Antibody Reactions Binding Sites, Antibody Biological markers Brachyura Contractile proteins Fluorescent Antibody Technique Horseradish Marine Microscopy, Phase-Contrast Models, Biological Molecules Muscle Proteins - analysis Muscles Muscles - analysis Mustard Plant - enzymology Myofibrils Myosins - analysis Peroxidases - pharmacology Plants, Medicinal Precipitin Tests Rabbits - immunology Sarcomeres Solar fibrils Staining and Labeling Striated muscle |
| title | Immunohistochemical Localization of Contractile Proteins in Limulus Striated Muscle |
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