Binding of nucleotides ATP and ADP to sarcoplasmic reticulm: study by rate of dialysis
Binding of the nucleotides ATP and ADP by preparations of sarcoplasmic reticulum was investigated by the method of flow dialysis. For ATP, experimental data could not be analyzed directly in terms of binding since a significant though small amount of hydrolysis could be observed even in presence of...
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| Veröffentlicht in: | Biochimie 1976, Vol.58 (5), p.513-519 |
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| container_title | Biochimie |
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| creator | Tenu, J P Ghelis, C Yon, J CHevallier, J |
| description | Binding of the nucleotides ATP and ADP by preparations of sarcoplasmic reticulum was investigated by the method of flow dialysis. For ATP, experimental data could not be analyzed directly in terms of binding since a significant though small amount of hydrolysis could be observed even in presence of EDTA. ADP binding could be analyzed and gave a dissociation constant of 10-20 muM at neutral pH, and a stoichiometry of 0.35 - 0.45 per mole ATPase. The possible significance of this stoichiometry is discussed. Similar experiments were performed after ethoxyformylation of sarcoplasmic reticulum which inhibits the Ca2+ dependnet ATPase activity. The results confirmed the inhibition of ATP hydrolysis and pointed to a considerably reduced affinity for nucleotides. The method based on the measurement of dialysis rates is convenient, and accurate enough to detect the effects of chemical modification on sarcoplasmic reticulum membranes. |
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For ATP, experimental data could not be analyzed directly in terms of binding since a significant though small amount of hydrolysis could be observed even in presence of EDTA. ADP binding could be analyzed and gave a dissociation constant of 10-20 muM at neutral pH, and a stoichiometry of 0.35 - 0.45 per mole ATPase. The possible significance of this stoichiometry is discussed. Similar experiments were performed after ethoxyformylation of sarcoplasmic reticulum which inhibits the Ca2+ dependnet ATPase activity. The results confirmed the inhibition of ATP hydrolysis and pointed to a considerably reduced affinity for nucleotides. The method based on the measurement of dialysis rates is convenient, and accurate enough to detect the effects of chemical modification on sarcoplasmic reticulum membranes.</description><identifier>ISSN: 0300-9084</identifier><identifier>PMID: 953055</identifier><language>eng</language><publisher>France</publisher><subject>Adenosine Diphosphate - metabolism ; Adenosine Triphosphate - metabolism ; Animals ; Binding Sites ; Biological Transport, Active ; Calcium - metabolism ; Dialysis ; Ethyl Ethers ; Kinetics ; Magnesium - metabolism ; Muscles - metabolism ; Protein Binding ; Rabbits ; Sarcoplasmic Reticulum - metabolism</subject><ispartof>Biochimie, 1976, Vol.58 (5), p.513-519</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/953055$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tenu, J P</creatorcontrib><creatorcontrib>Ghelis, C</creatorcontrib><creatorcontrib>Yon, J</creatorcontrib><creatorcontrib>CHevallier, J</creatorcontrib><title>Binding of nucleotides ATP and ADP to sarcoplasmic reticulm: study by rate of dialysis</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>Binding of the nucleotides ATP and ADP by preparations of sarcoplasmic reticulum was investigated by the method of flow dialysis. For ATP, experimental data could not be analyzed directly in terms of binding since a significant though small amount of hydrolysis could be observed even in presence of EDTA. ADP binding could be analyzed and gave a dissociation constant of 10-20 muM at neutral pH, and a stoichiometry of 0.35 - 0.45 per mole ATPase. The possible significance of this stoichiometry is discussed. Similar experiments were performed after ethoxyformylation of sarcoplasmic reticulum which inhibits the Ca2+ dependnet ATPase activity. The results confirmed the inhibition of ATP hydrolysis and pointed to a considerably reduced affinity for nucleotides. The method based on the measurement of dialysis rates is convenient, and accurate enough to detect the effects of chemical modification on sarcoplasmic reticulum membranes.</description><subject>Adenosine Diphosphate - metabolism</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biological Transport, Active</subject><subject>Calcium - metabolism</subject><subject>Dialysis</subject><subject>Ethyl Ethers</subject><subject>Kinetics</subject><subject>Magnesium - metabolism</subject><subject>Muscles - metabolism</subject><subject>Protein Binding</subject><subject>Rabbits</subject><subject>Sarcoplasmic Reticulum - metabolism</subject><issn>0300-9084</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNotkDlPwzAYQD1wlcI_YPDEFunz1cZsoZxSJTpErJHjAxk5cbDjIf8eUDu95ekN7wytgAFUEmp-ha5z_gYAAVReogspGAixQp-PfjR-_MLR4bHoYOPsjc24aQ9YjQY3Twc8R5xV0nEKKg9e42Rnr0sYHnCei1lwv-CkZvufMF6FJft8g86dCtnenrhG7ctzu3ur9h-v77tmX02CiooKroVzWjrNhFW9JNBTLm1NZK31xvCtEVsgnBtWO-KoIVwTpjaUM0uZArZG98fslOJPsXnuBp-1DUGNNpbc1YxTyqn8E-9OYukHa7op-UGlpTtuYL-59Fc9</recordid><startdate>1976</startdate><enddate>1976</enddate><creator>Tenu, J P</creator><creator>Ghelis, C</creator><creator>Yon, J</creator><creator>CHevallier, J</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>1976</creationdate><title>Binding of nucleotides ATP and ADP to sarcoplasmic reticulm: study by rate of dialysis</title><author>Tenu, J P ; Ghelis, C ; Yon, J ; CHevallier, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p525-254c5ffc9fc35eab910b249e8198cc6d47d570144d38f1f2d14c13a6243e23a03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Adenosine Diphosphate - metabolism</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Biological Transport, Active</topic><topic>Calcium - metabolism</topic><topic>Dialysis</topic><topic>Ethyl Ethers</topic><topic>Kinetics</topic><topic>Magnesium - metabolism</topic><topic>Muscles - metabolism</topic><topic>Protein Binding</topic><topic>Rabbits</topic><topic>Sarcoplasmic Reticulum - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tenu, J P</creatorcontrib><creatorcontrib>Ghelis, C</creatorcontrib><creatorcontrib>Yon, J</creatorcontrib><creatorcontrib>CHevallier, J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tenu, J P</au><au>Ghelis, C</au><au>Yon, J</au><au>CHevallier, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Binding of nucleotides ATP and ADP to sarcoplasmic reticulm: study by rate of dialysis</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>1976</date><risdate>1976</risdate><volume>58</volume><issue>5</issue><spage>513</spage><epage>519</epage><pages>513-519</pages><issn>0300-9084</issn><abstract>Binding of the nucleotides ATP and ADP by preparations of sarcoplasmic reticulum was investigated by the method of flow dialysis. For ATP, experimental data could not be analyzed directly in terms of binding since a significant though small amount of hydrolysis could be observed even in presence of EDTA. ADP binding could be analyzed and gave a dissociation constant of 10-20 muM at neutral pH, and a stoichiometry of 0.35 - 0.45 per mole ATPase. The possible significance of this stoichiometry is discussed. Similar experiments were performed after ethoxyformylation of sarcoplasmic reticulum which inhibits the Ca2+ dependnet ATPase activity. The results confirmed the inhibition of ATP hydrolysis and pointed to a considerably reduced affinity for nucleotides. The method based on the measurement of dialysis rates is convenient, and accurate enough to detect the effects of chemical modification on sarcoplasmic reticulum membranes.</abstract><cop>France</cop><pmid>953055</pmid><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0300-9084 |
| ispartof | Biochimie, 1976, Vol.58 (5), p.513-519 |
| issn | 0300-9084 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Adenosine Diphosphate - metabolism Adenosine Triphosphate - metabolism Animals Binding Sites Biological Transport, Active Calcium - metabolism Dialysis Ethyl Ethers Kinetics Magnesium - metabolism Muscles - metabolism Protein Binding Rabbits Sarcoplasmic Reticulum - metabolism |
| title | Binding of nucleotides ATP and ADP to sarcoplasmic reticulm: study by rate of dialysis |
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