Adjustment of K' for the creatine kinase, adenylate kinase and ATP hydrolysis equilibria to varying temperature and ionic strength
Comparative physiologists and biochemists working with tissues at varying temperatures and ionic strength are required to adjust apparent equilibrium constants (K') of biochemical reactions to the experimental conditions prior to calculating cytosolic bioenergetic parameters (transformed Gibbs...
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| Veröffentlicht in: | Journal of experimental biology 1996-02, Vol.199 (Pt 2), p.509-512 |
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| container_end_page | 512 |
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| container_issue | Pt 2 |
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| container_title | Journal of experimental biology |
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| creator | Teague, Jr, W E Golding, E M Dobson, G P |
| description | Comparative physiologists and biochemists working with tissues at varying temperatures and ionic strength are required to adjust apparent equilibrium constants (K') of biochemical reactions to the experimental conditions prior to calculating cytosolic bioenergetic parameters (transformed Gibbs free energy of formation, DeltafG' ATP; cytosolic phosphorylation ratio, [ATP]/[ADP][Pi]; [phosphocreatine]: [orthophosphate] ratio [PCr]/[Pi]) and kinetic parameters (free [ADP], [Pi] and [AMP]). The present study shows how to adjust both K' and the equilibrium constants of reference reactions (Kref) of creatine kinase (ATP: creatine N-phosphotransferase; EC 2.7.3.2), adenylate kinase (ATP:AMP phosphotransferase; EC 2.7.4.3) and adenosinetriphosphatase (ATP phosphohydrolase; EC 3.6.1.3) to temperature and ionic strength. This information, together with our previous study showing how to adjust equilibria to varying pH and pMg, is vital for the quantification of organ and tissue bioenergetics of ectotherms and endotherms under physiological conditions. |
| doi_str_mv | 10.1242/jeb.199.2.509 |
| format | Article |
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The present study shows how to adjust both K' and the equilibrium constants of reference reactions (Kref) of creatine kinase (ATP: creatine N-phosphotransferase; EC 2.7.3.2), adenylate kinase (ATP:AMP phosphotransferase; EC 2.7.4.3) and adenosinetriphosphatase (ATP phosphohydrolase; EC 3.6.1.3) to temperature and ionic strength. 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The present study shows how to adjust both K' and the equilibrium constants of reference reactions (Kref) of creatine kinase (ATP: creatine N-phosphotransferase; EC 2.7.3.2), adenylate kinase (ATP:AMP phosphotransferase; EC 2.7.4.3) and adenosinetriphosphatase (ATP phosphohydrolase; EC 3.6.1.3) to temperature and ionic strength. This information, together with our previous study showing how to adjust equilibria to varying pH and pMg, is vital for the quantification of organ and tissue bioenergetics of ectotherms and endotherms under physiological conditions.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Adenylate Kinase - metabolism</subject><subject>Animals</subject><subject>Biology</subject><subject>Creatine Kinase - metabolism</subject><subject>Energy Metabolism</subject><subject>Kinetics</subject><subject>Measurement</subject><subject>Models, Biological</subject><subject>Osmolar Concentration</subject><subject>Temperature</subject><subject>Vertebrates</subject><issn>0022-0949</issn><issn>1477-9145</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUtP3DAQgK0KRBfokSOSxaFcmq0fcRIfV6gPBFJ7gLNlJ2PWS2IvtlNpr_zyGu2WQ-cyo9E3oxl9CF1QsqSsZl83YJZUyiVbCiI_oAWt27aStBZHaEEIYxWRtfyITlPakBKNqE_QSSd5qfkCva6GzZzyBD7jYPHdNbYh4rwG3EfQ2XnAz87rBF-wHsDvRp3_dbD2A149_Mbr3RDDuEsuYXiZ3ehMdBrngP_ouHP-CWeYthB1nuN-yAXvepxyBP-U1-fo2OoxwadDPkOP37893Pys7n_9uL1Z3Vc9FzRXVgqgfdPTtjPMtNKatrMGamMN5QC6sc3Q9VY0LXAyMAqWcEmH2lIiGs04P0Of93u3MbzMkLKaXOphHLWHMCfVdqJuaPcGXv0HbsIcfblNMU44E13LClTtoT6GlCJYtY1uKg8rStSbGFXEqCJGMVXEFP7ysHQ2Ewzv9MEE_wt55Isf</recordid><startdate>199602</startdate><enddate>199602</enddate><creator>Teague, Jr, W E</creator><creator>Golding, E M</creator><creator>Dobson, G P</creator><general>The Company of Biologists Ltd</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>7QG</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7TK</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>199602</creationdate><title>Adjustment of K' for the creatine kinase, adenylate kinase and ATP hydrolysis equilibria to varying temperature and ionic strength</title><author>Teague, Jr, W E ; Golding, E M ; Dobson, G P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c351t-f95e1c6c178b2b79fb78fbe4bfb13eea6f6d8cf567e30d21ef0391d4f1056a233</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Adenylate Kinase - metabolism</topic><topic>Animals</topic><topic>Biology</topic><topic>Creatine Kinase - metabolism</topic><topic>Energy Metabolism</topic><topic>Kinetics</topic><topic>Measurement</topic><topic>Models, Biological</topic><topic>Osmolar Concentration</topic><topic>Temperature</topic><topic>Vertebrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Teague, Jr, W E</creatorcontrib><creatorcontrib>Golding, E M</creatorcontrib><creatorcontrib>Dobson, G P</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of experimental biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Teague, Jr, W E</au><au>Golding, E M</au><au>Dobson, G P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Adjustment of K' for the creatine kinase, adenylate kinase and ATP hydrolysis equilibria to varying temperature and ionic strength</atitle><jtitle>Journal of experimental biology</jtitle><addtitle>J Exp Biol</addtitle><date>1996-02</date><risdate>1996</risdate><volume>199</volume><issue>Pt 2</issue><spage>509</spage><epage>512</epage><pages>509-512</pages><issn>0022-0949</issn><eissn>1477-9145</eissn><coden>JEBIAM</coden><abstract>Comparative physiologists and biochemists working with tissues at varying temperatures and ionic strength are required to adjust apparent equilibrium constants (K') of biochemical reactions to the experimental conditions prior to calculating cytosolic bioenergetic parameters (transformed Gibbs free energy of formation, DeltafG' ATP; cytosolic phosphorylation ratio, [ATP]/[ADP][Pi]; [phosphocreatine]: [orthophosphate] ratio [PCr]/[Pi]) and kinetic parameters (free [ADP], [Pi] and [AMP]). The present study shows how to adjust both K' and the equilibrium constants of reference reactions (Kref) of creatine kinase (ATP: creatine N-phosphotransferase; EC 2.7.3.2), adenylate kinase (ATP:AMP phosphotransferase; EC 2.7.4.3) and adenosinetriphosphatase (ATP phosphohydrolase; EC 3.6.1.3) to temperature and ionic strength. This information, together with our previous study showing how to adjust equilibria to varying pH and pMg, is vital for the quantification of organ and tissue bioenergetics of ectotherms and endotherms under physiological conditions.</abstract><cop>England</cop><pub>The Company of Biologists Ltd</pub><pmid>8930003</pmid><doi>10.1242/jeb.199.2.509</doi><tpages>4</tpages></addata></record> |
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| ispartof | Journal of experimental biology, 1996-02, Vol.199 (Pt 2), p.509-512 |
| issn | 0022-0949 1477-9145 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Company of Biologists |
| subjects | Adenosine Triphosphate - metabolism Adenylate Kinase - metabolism Animals Biology Creatine Kinase - metabolism Energy Metabolism Kinetics Measurement Models, Biological Osmolar Concentration Temperature Vertebrates |
| title | Adjustment of K' for the creatine kinase, adenylate kinase and ATP hydrolysis equilibria to varying temperature and ionic strength |
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