Interaction of Tropomyosin with Troponin Components

1. The TN-T and TN-I components of troponin both interact with tropomyosin and cause its precipitation in 0.1 M KCl at neutral pH. The precipitate contains both end-to-end and side-by-side aggregates of tropomyosin molecules. 2. The TN-T and TN-I components change the band pattern of tropomyosin par...

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Veröffentlicht in:	Journal of biochemistry (Tokyo) 1976-07, Vol.80 (1), p.89-99
Hauptverfasser:	DABROWSKA, Renata, PODLUBNAYA, Zoya, NOWAK, Ewa, DRABIKOWSKI, Witold
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Crystallization Hydrogen-Ion Concentration Magnesium Microscopy, Electron Muscle Proteins Potassium Chloride Protein Binding Protein Conformation Rabbits Tropomyosin Troponin
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container_title	Journal of biochemistry (Tokyo)
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creator	DABROWSKA, Renata PODLUBNAYA, Zoya NOWAK, Ewa DRABIKOWSKI, Witold
description	1. The TN-T and TN-I components of troponin both interact with tropomyosin and cause its precipitation in 0.1 M KCl at neutral pH. The precipitate contains both end-to-end and side-by-side aggregates of tropomyosin molecules. 2. The TN-T and TN-I components change the band pattern of tropomyosin paracrystals formed in MgCl2 solutions, although in different ways. TN-T causes the formation of hexagonal net structures, double-stranded net or paracrystals which result from the collapse of the double-stranded net. TN-I at pH 7.9 causes the formation of paracrystals with a 400 A periodic band pattern and a 200 A repeat. The same band pattern can also be seen in tropomyosin paracrystals formed at pH values below 6.0. 3. The TN-C component does not precipitate tropomyosin in 0.1 M KCl. The aggregates of tropomyosin obtained with either TN-T or TN-I can be solubilized by the addition of TN-C. No interaction of TN-C was observed with tropomyosin paracrystals formed in the presence of MgCl2.
doi_str_mv	10.1093/oxfordjournals.jbchem.a131262
format	Article
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The TN-T and TN-I components of troponin both interact with tropomyosin and cause its precipitation in 0.1 M KCl at neutral pH. The precipitate contains both end-to-end and side-by-side aggregates of tropomyosin molecules. 2. The TN-T and TN-I components change the band pattern of tropomyosin paracrystals formed in MgCl2 solutions, although in different ways. TN-T causes the formation of hexagonal net structures, double-stranded net or paracrystals which result from the collapse of the double-stranded net. TN-I at pH 7.9 causes the formation of paracrystals with a 400 A periodic band pattern and a 200 A repeat. The same band pattern can also be seen in tropomyosin paracrystals formed at pH values below 6.0. 3. The TN-C component does not precipitate tropomyosin in 0.1 M KCl. The aggregates of tropomyosin obtained with either TN-T or TN-I can be solubilized by the addition of TN-C. No interaction of TN-C was observed with tropomyosin paracrystals formed in the presence of MgCl2.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a131262</identifier><identifier>PMID: 9383</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Animals ; Crystallization ; Hydrogen-Ion Concentration ; Magnesium ; Microscopy, Electron ; Muscle Proteins ; Potassium Chloride ; Protein Binding ; Protein Conformation ; Rabbits ; Tropomyosin ; Troponin</subject><ispartof>Journal of biochemistry (Tokyo), 1976-07, Vol.80 (1), p.89-99</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c355t-12aba96783ed0ad44dd357295ca68dd18e102753db80b0c4fad0a947a072098a3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9383$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>DABROWSKA, Renata</creatorcontrib><creatorcontrib>PODLUBNAYA, Zoya</creatorcontrib><creatorcontrib>NOWAK, Ewa</creatorcontrib><creatorcontrib>DRABIKOWSKI, Witold</creatorcontrib><title>Interaction of Tropomyosin with Troponin Components</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>1. The TN-T and TN-I components of troponin both interact with tropomyosin and cause its precipitation in 0.1 M KCl at neutral pH. The precipitate contains both end-to-end and side-by-side aggregates of tropomyosin molecules. 2. The TN-T and TN-I components change the band pattern of tropomyosin paracrystals formed in MgCl2 solutions, although in different ways. TN-T causes the formation of hexagonal net structures, double-stranded net or paracrystals which result from the collapse of the double-stranded net. TN-I at pH 7.9 causes the formation of paracrystals with a 400 A periodic band pattern and a 200 A repeat. The same band pattern can also be seen in tropomyosin paracrystals formed at pH values below 6.0. 3. The TN-C component does not precipitate tropomyosin in 0.1 M KCl. The aggregates of tropomyosin obtained with either TN-T or TN-I can be solubilized by the addition of TN-C. No interaction of TN-C was observed with tropomyosin paracrystals formed in the presence of MgCl2.</description><subject>Animals</subject><subject>Crystallization</subject><subject>Hydrogen-Ion Concentration</subject><subject>Magnesium</subject><subject>Microscopy, Electron</subject><subject>Muscle Proteins</subject><subject>Potassium Chloride</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Rabbits</subject><subject>Tropomyosin</subject><subject>Troponin</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkMtOwzAQRS1UBKXwA6y6gV2C7YkfWbBA5dFKFWyKVLGxnNhRU5q42Ilo_55UqSqxmsedmas5CN0RHBOcwoPbFc6btWt9rTchXmf5ylaxJkAop2doSATjEeWMDNAQY0qilCbLS3QVwvpQUoALNEhBwhDBrG6s13lTunrsivHCu62r9i6U9fi3bFZ9o-6qiau6xNZNuEbnRedrb45xhD5fXxaTaTT_eJtNnuZRDow1EaE60ykXEqzB2iSJMcAETVmuuTSGSEswFQxMJnGG86TQ3ViaCI0FxanUMEL3_d2tdz-tDY2qypDbzUbX1rVBSUg4QPfGCD32g7l3IXhbqK0vK-33imB1IKb-E1M9MXUk1u3fHo3arLLmtH1A1IlRL5ahsbuTpv234gIEU9Pll5J8IZ6BvKsE_gCQm348</recordid><startdate>197607</startdate><enddate>197607</enddate><creator>DABROWSKA, Renata</creator><creator>PODLUBNAYA, Zoya</creator><creator>NOWAK, Ewa</creator><creator>DRABIKOWSKI, Witold</creator><general>Oxford University Press</general><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>7X8</scope></search><sort><creationdate>197607</creationdate><title>Interaction of Tropomyosin with Troponin Components</title><author>DABROWSKA, Renata ; PODLUBNAYA, Zoya ; NOWAK, Ewa ; DRABIKOWSKI, Witold</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c355t-12aba96783ed0ad44dd357295ca68dd18e102753db80b0c4fad0a947a072098a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Animals</topic><topic>Crystallization</topic><topic>Hydrogen-Ion Concentration</topic><topic>Magnesium</topic><topic>Microscopy, Electron</topic><topic>Muscle Proteins</topic><topic>Potassium Chloride</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Rabbits</topic><topic>Tropomyosin</topic><topic>Troponin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>DABROWSKA, Renata</creatorcontrib><creatorcontrib>PODLUBNAYA, Zoya</creatorcontrib><creatorcontrib>NOWAK, Ewa</creatorcontrib><creatorcontrib>DRABIKOWSKI, Witold</creatorcontrib><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>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>DABROWSKA, Renata</au><au>PODLUBNAYA, Zoya</au><au>NOWAK, Ewa</au><au>DRABIKOWSKI, Witold</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of Tropomyosin with Troponin Components</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1976-07</date><risdate>1976</risdate><volume>80</volume><issue>1</issue><spage>89</spage><epage>99</epage><pages>89-99</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>1. The TN-T and TN-I components of troponin both interact with tropomyosin and cause its precipitation in 0.1 M KCl at neutral pH. The precipitate contains both end-to-end and side-by-side aggregates of tropomyosin molecules. 2. The TN-T and TN-I components change the band pattern of tropomyosin paracrystals formed in MgCl2 solutions, although in different ways. TN-T causes the formation of hexagonal net structures, double-stranded net or paracrystals which result from the collapse of the double-stranded net. TN-I at pH 7.9 causes the formation of paracrystals with a 400 A periodic band pattern and a 200 A repeat. The same band pattern can also be seen in tropomyosin paracrystals formed at pH values below 6.0. 3. The TN-C component does not precipitate tropomyosin in 0.1 M KCl. The aggregates of tropomyosin obtained with either TN-T or TN-I can be solubilized by the addition of TN-C. No interaction of TN-C was observed with tropomyosin paracrystals formed in the presence of MgCl2.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>9383</pmid><doi>10.1093/oxfordjournals.jbchem.a131262</doi><tpages>11</tpages></addata></record>
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subjects	Animals Crystallization Hydrogen-Ion Concentration Magnesium Microscopy, Electron Muscle Proteins Potassium Chloride Protein Binding Protein Conformation Rabbits Tropomyosin Troponin
title	Interaction of Tropomyosin with Troponin Components
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