Ordering of the myofilament lattice in muscle fibers
The effect of pH on the muscle filament lattice in skinned rabbit psoas fibers was studied by X-ray diffraction. In relaxed fibers, the intensity of the 11 equatorial reflection, I 11, remained constant between pH 7.0 and pH 6.0 and fell markedly when the pH was decreased to 5.5. The intensity of th...
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| Veröffentlicht in: | Journal of molecular biology 1986-05, Vol.189 (2), p.361-365 |
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| creator | Matsuda, Takashi Podolsky, Richard J. |
| description | The effect of pH on the muscle filament lattice in skinned rabbit psoas fibers was studied by X-ray diffraction. In relaxed fibers, the intensity of the 11 equatorial reflection,
I
11, remained constant between pH 7.0 and pH 6.0 and fell markedly when the pH was decreased to 5.5. The intensity of the 10 reflection was almost constant over this pH range. These results indicate that the thick-filament lattice is more stable than that of the thin filaments, and that the thin filaments are positioned within the thick-filament lattice by a charge-dependent force. In rigor fibers, the decrease in
I
11 over this pH range was much smaller, which shows that the thin filament lattice can also be stabilized by the presence of actomyosin crossbridges. These conclusions were confirmed by electron microscopy. Thus, the thin filaments can be positioned in the trigonal positions of the thick-filament lattice by two different mechanisms, one electrostatic and the other steric. |
| doi_str_mv | 10.1016/0022-2836(86)90516-4 |
| format | Article |
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I
11, remained constant between pH 7.0 and pH 6.0 and fell markedly when the pH was decreased to 5.5. The intensity of the 10 reflection was almost constant over this pH range. These results indicate that the thick-filament lattice is more stable than that of the thin filaments, and that the thin filaments are positioned within the thick-filament lattice by a charge-dependent force. In rigor fibers, the decrease in
I
11 over this pH range was much smaller, which shows that the thin filament lattice can also be stabilized by the presence of actomyosin crossbridges. These conclusions were confirmed by electron microscopy. Thus, the thin filaments can be positioned in the trigonal positions of the thick-filament lattice by two different mechanisms, one electrostatic and the other steric.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/0022-2836(86)90516-4</identifier><identifier>PMID: 3746912</identifier><identifier>CODEN: JMOBAK</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Actin Cytoskeleton - ultrastructure ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Contractile proteins ; Cytoskeleton - ultrastructure ; Fundamental and applied biological sciences. Psychology ; Holoproteins ; Hydrogen-Ion Concentration ; Microscopy, Electron ; Muscle Contraction ; Muscle Relaxation ; Muscles - ultrastructure ; Proteins ; Rabbits ; X-Ray Diffraction</subject><ispartof>Journal of molecular biology, 1986-05, Vol.189 (2), p.361-365</ispartof><rights>1986</rights><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-f5e333670ca12c5cb7667937d00b1c0fa56a214e85571d50396c3c46a89b3cd93</citedby><cites>FETCH-LOGICAL-c386t-f5e333670ca12c5cb7667937d00b1c0fa56a214e85571d50396c3c46a89b3cd93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0022-2836(86)90516-4$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3541,27915,27916,45986</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8711396$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3746912$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Matsuda, Takashi</creatorcontrib><creatorcontrib>Podolsky, Richard J.</creatorcontrib><title>Ordering of the myofilament lattice in muscle fibers</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>The effect of pH on the muscle filament lattice in skinned rabbit psoas fibers was studied by X-ray diffraction. In relaxed fibers, the intensity of the 11 equatorial reflection,
I
11, remained constant between pH 7.0 and pH 6.0 and fell markedly when the pH was decreased to 5.5. The intensity of the 10 reflection was almost constant over this pH range. These results indicate that the thick-filament lattice is more stable than that of the thin filaments, and that the thin filaments are positioned within the thick-filament lattice by a charge-dependent force. In rigor fibers, the decrease in
I
11 over this pH range was much smaller, which shows that the thin filament lattice can also be stabilized by the presence of actomyosin crossbridges. These conclusions were confirmed by electron microscopy. Thus, the thin filaments can be positioned in the trigonal positions of the thick-filament lattice by two different mechanisms, one electrostatic and the other steric.</description><subject>Actin Cytoskeleton - ultrastructure</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Contractile proteins</subject><subject>Cytoskeleton - ultrastructure</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Holoproteins</subject><subject>Hydrogen-Ion Concentration</subject><subject>Microscopy, Electron</subject><subject>Muscle Contraction</subject><subject>Muscle Relaxation</subject><subject>Muscles - ultrastructure</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>X-Ray Diffraction</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLAzEUhYMotVb_gcIsRHQxmkwySWYjSPEFhW50HTJ3bjQyj5rMCP33Tm3p0tVdnO8cLh8h54zeMsrkHaVZlmaay2stbwqaM5mKAzJlVBepllwfkukeOSYnMX5RSnMu9IRMuBKyYNmUiGWoMPj2I-lc0n9i0qw752vbYNsnte17D5j4NmmGCDUmzpcY4ik5craOeLa7M_L-9Pg2f0kXy-fX-cMiBa5ln7ocOedSUbAsgxxKJaUquKooLRlQZ3NpMyZQ57liVU55IYGDkFYXJYeq4DNytd1dhe57wNibxkfAurYtdkM0StHRhNIjKLYghC7GgM6sgm9sWBtGzUaW2ZgwGxNGS_Mny4ixdrHbH8oGq31pZ2fML3e5jWBrF2wLPu4xrRgbfx6x-y2Go4sfj8FE8NgCVj4g9Kbq_P9__AJ1g4OC</recordid><startdate>19860520</startdate><enddate>19860520</enddate><creator>Matsuda, Takashi</creator><creator>Podolsky, Richard J.</creator><general>Elsevier Ltd</general><general>Elsevier</general><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>19860520</creationdate><title>Ordering of the myofilament lattice in muscle fibers</title><author>Matsuda, Takashi ; Podolsky, Richard J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-f5e333670ca12c5cb7667937d00b1c0fa56a214e85571d50396c3c46a89b3cd93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Actin Cytoskeleton - ultrastructure</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Contractile proteins</topic><topic>Cytoskeleton - ultrastructure</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Holoproteins</topic><topic>Hydrogen-Ion Concentration</topic><topic>Microscopy, Electron</topic><topic>Muscle Contraction</topic><topic>Muscle Relaxation</topic><topic>Muscles - ultrastructure</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Matsuda, Takashi</creatorcontrib><creatorcontrib>Podolsky, Richard J.</creatorcontrib><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>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Matsuda, Takashi</au><au>Podolsky, Richard J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ordering of the myofilament lattice in muscle fibers</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1986-05-20</date><risdate>1986</risdate><volume>189</volume><issue>2</issue><spage>361</spage><epage>365</epage><pages>361-365</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>The effect of pH on the muscle filament lattice in skinned rabbit psoas fibers was studied by X-ray diffraction. In relaxed fibers, the intensity of the 11 equatorial reflection,
I
11, remained constant between pH 7.0 and pH 6.0 and fell markedly when the pH was decreased to 5.5. The intensity of the 10 reflection was almost constant over this pH range. These results indicate that the thick-filament lattice is more stable than that of the thin filaments, and that the thin filaments are positioned within the thick-filament lattice by a charge-dependent force. In rigor fibers, the decrease in
I
11 over this pH range was much smaller, which shows that the thin filament lattice can also be stabilized by the presence of actomyosin crossbridges. These conclusions were confirmed by electron microscopy. Thus, the thin filaments can be positioned in the trigonal positions of the thick-filament lattice by two different mechanisms, one electrostatic and the other steric.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>3746912</pmid><doi>10.1016/0022-2836(86)90516-4</doi><tpages>5</tpages></addata></record> |
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| subjects | Actin Cytoskeleton - ultrastructure Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Contractile proteins Cytoskeleton - ultrastructure Fundamental and applied biological sciences. Psychology Holoproteins Hydrogen-Ion Concentration Microscopy, Electron Muscle Contraction Muscle Relaxation Muscles - ultrastructure Proteins Rabbits X-Ray Diffraction |
| title | Ordering of the myofilament lattice in muscle fibers |
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