Regulatory proteins of lobster striated muscle
The regulatory proteins of lobster muscles consist of tropomyosin and of troponin. Troponin contains a 17,000 chain weight component, two closely related components of about 30,000 and a 52,000 chain weight component. In addition to troponin, tropomyosin is required for the inhibition of the magnesi...
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| Veröffentlicht in: | Biochemistry (Easton) 1975-03, Vol.14 (5), p.917-925 |
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| container_title | Biochemistry (Easton) |
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| creator | Regenstein, Joe M Szent-Gyorgyi, Andrew G |
| description | The regulatory proteins of lobster muscles consist of tropomyosin and of troponin. Troponin contains a 17,000 chain weight component, two closely related components of about 30,000 and a 52,000 chain weight component. In addition to troponin, tropomyosin is required for the inhibition of the magnesium activated actomyosin ATPase activity in the absence of calcium and for the reversal of this inhibition by calcium. Lobster tropomyosin interacts with rabbit actin and lobster troponin interacts with rabbit tropomyosin. The 30,000 doublet component corresponds to the troponin-I of rabbit and inhibits the ATPase activity of actomyosin both in the presence and in the absence of calcium. The 17,000 component corresponds to the troponin-C of rabbit; it binds calcium and reverses the inhibition of the ATPase activity by troponin-I in the presence of calcium. No more than 1 mol of calcium is bound by a mole of troponin-C or by troponin. The 52,000 component interacts with tropomyosin and has been tentatively identified as troponin-T; however, it has not been demonstrated as yet that this component had a role in the regulation of lobster actomyosin. |
| doi_str_mv | 10.1021/bi00676a007 |
| format | Article |
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Troponin contains a 17,000 chain weight component, two closely related components of about 30,000 and a 52,000 chain weight component. In addition to troponin, tropomyosin is required for the inhibition of the magnesium activated actomyosin ATPase activity in the absence of calcium and for the reversal of this inhibition by calcium. Lobster tropomyosin interacts with rabbit actin and lobster troponin interacts with rabbit tropomyosin. The 30,000 doublet component corresponds to the troponin-I of rabbit and inhibits the ATPase activity of actomyosin both in the presence and in the absence of calcium. The 17,000 component corresponds to the troponin-C of rabbit; it binds calcium and reverses the inhibition of the ATPase activity by troponin-I in the presence of calcium. No more than 1 mol of calcium is bound by a mole of troponin-C or by troponin. The 52,000 component interacts with tropomyosin and has been tentatively identified as troponin-T; however, it has not been demonstrated as yet that this component had a role in the regulation of lobster actomyosin.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00676a007</identifier><identifier>PMID: 123757</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Actomyosin - metabolism ; Adenosine Triphosphatases - metabolism ; Amino Acids - analysis ; Animals ; Binding Sites ; Binding, Competitive ; Calcium - pharmacology ; Enzyme Activation - drug effects ; Kinetics ; Macromolecular Substances ; Magnesium - pharmacology ; Molecular Weight ; Muscle Proteins - metabolism ; Muscles - metabolism ; Nephropidae ; Protein Binding ; Rabbits ; Tropomyosin - metabolism ; Troponin - metabolism</subject><ispartof>Biochemistry (Easton), 1975-03, Vol.14 (5), p.917-925</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a419t-8978acdd8b8c21d02108022ab49629f6cd067d560f4ed1993ef5a8d8a94422b93</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00676a007$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00676a007$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/123757$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Regenstein, Joe M</creatorcontrib><creatorcontrib>Szent-Gyorgyi, Andrew G</creatorcontrib><title>Regulatory proteins of lobster striated muscle</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The regulatory proteins of lobster muscles consist of tropomyosin and of troponin. Troponin contains a 17,000 chain weight component, two closely related components of about 30,000 and a 52,000 chain weight component. In addition to troponin, tropomyosin is required for the inhibition of the magnesium activated actomyosin ATPase activity in the absence of calcium and for the reversal of this inhibition by calcium. Lobster tropomyosin interacts with rabbit actin and lobster troponin interacts with rabbit tropomyosin. The 30,000 doublet component corresponds to the troponin-I of rabbit and inhibits the ATPase activity of actomyosin both in the presence and in the absence of calcium. The 17,000 component corresponds to the troponin-C of rabbit; it binds calcium and reverses the inhibition of the ATPase activity by troponin-I in the presence of calcium. No more than 1 mol of calcium is bound by a mole of troponin-C or by troponin. The 52,000 component interacts with tropomyosin and has been tentatively identified as troponin-T; however, it has not been demonstrated as yet that this component had a role in the regulation of lobster actomyosin.</description><subject>Actomyosin - metabolism</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Binding, Competitive</subject><subject>Calcium - pharmacology</subject><subject>Enzyme Activation - drug effects</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>Magnesium - pharmacology</subject><subject>Molecular Weight</subject><subject>Muscle Proteins - metabolism</subject><subject>Muscles - metabolism</subject><subject>Nephropidae</subject><subject>Protein Binding</subject><subject>Rabbits</subject><subject>Tropomyosin - metabolism</subject><subject>Troponin - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkDtPwzAUhS3EqxQmVoZMMKAU23X8GEt5lkpUUGbLiR2UktTFdiT67zGkAgamq6vz6dxzDwDHCA4QxOgiryCkjCoI2RbooQzDlAiRbYMejEKKBYX74MD7RVwJZGQP7CI8ZBnrgcGTeW1rFaxbJytng6mWPrFlUtvcB-MSH1ylgtFJ0_qiNodgp1S1N0eb2QcvN9fz8V06fby9H4-mqSJIhJQLxlWhNc95gZGOGSGHGKucCIpFSQsd8-qMwpIYjYQYmjJTXHMlCME4F8M-OO18Y6b31vggm8oXpq7V0tjWS4654JjiCJ53YOGs986UcuWqRrm1RFB-lSP_lBPpk41tmzdG_7LfbUQ57eQq_v7xoyr3JimLhJzPniWeXE6uHuhEziJ_1vGq8HJhW7eMnfx7-BPBjnlX</recordid><startdate>19750311</startdate><enddate>19750311</enddate><creator>Regenstein, Joe M</creator><creator>Szent-Gyorgyi, Andrew G</creator><general>American Chemical Society</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>19750311</creationdate><title>Regulatory proteins of lobster striated muscle</title><author>Regenstein, Joe M ; Szent-Gyorgyi, Andrew G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a419t-8978acdd8b8c21d02108022ab49629f6cd067d560f4ed1993ef5a8d8a94422b93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Actomyosin - metabolism</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Binding, Competitive</topic><topic>Calcium - pharmacology</topic><topic>Enzyme Activation - drug effects</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>Magnesium - pharmacology</topic><topic>Molecular Weight</topic><topic>Muscle Proteins - metabolism</topic><topic>Muscles - metabolism</topic><topic>Nephropidae</topic><topic>Protein Binding</topic><topic>Rabbits</topic><topic>Tropomyosin - metabolism</topic><topic>Troponin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Regenstein, Joe M</creatorcontrib><creatorcontrib>Szent-Gyorgyi, Andrew G</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>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Regenstein, Joe M</au><au>Szent-Gyorgyi, Andrew G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulatory proteins of lobster striated muscle</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1975-03-11</date><risdate>1975</risdate><volume>14</volume><issue>5</issue><spage>917</spage><epage>925</epage><pages>917-925</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The regulatory proteins of lobster muscles consist of tropomyosin and of troponin. Troponin contains a 17,000 chain weight component, two closely related components of about 30,000 and a 52,000 chain weight component. In addition to troponin, tropomyosin is required for the inhibition of the magnesium activated actomyosin ATPase activity in the absence of calcium and for the reversal of this inhibition by calcium. Lobster tropomyosin interacts with rabbit actin and lobster troponin interacts with rabbit tropomyosin. The 30,000 doublet component corresponds to the troponin-I of rabbit and inhibits the ATPase activity of actomyosin both in the presence and in the absence of calcium. The 17,000 component corresponds to the troponin-C of rabbit; it binds calcium and reverses the inhibition of the ATPase activity by troponin-I in the presence of calcium. No more than 1 mol of calcium is bound by a mole of troponin-C or by troponin. The 52,000 component interacts with tropomyosin and has been tentatively identified as troponin-T; however, it has not been demonstrated as yet that this component had a role in the regulation of lobster actomyosin.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>123757</pmid><doi>10.1021/bi00676a007</doi><tpages>9</tpages></addata></record> |
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| identifier | ISSN: 0006-2960 |
| ispartof | Biochemistry (Easton), 1975-03, Vol.14 (5), p.917-925 |
| issn | 0006-2960 1520-4995 |
| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Actomyosin - metabolism Adenosine Triphosphatases - metabolism Amino Acids - analysis Animals Binding Sites Binding, Competitive Calcium - pharmacology Enzyme Activation - drug effects Kinetics Macromolecular Substances Magnesium - pharmacology Molecular Weight Muscle Proteins - metabolism Muscles - metabolism Nephropidae Protein Binding Rabbits Tropomyosin - metabolism Troponin - metabolism |
| title | Regulatory proteins of lobster striated muscle |
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