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10.1023/b:jobb.0000031978.15139.49
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Lax Pérez, Antonio Manuel | - |
dc.contributor.author | Soler Pardo, Fernando | - |
dc.contributor.author | Fernandez Belda, Francisco | - |
dc.contributor.other | Facultades, Departamentos, Servicios y Escuelas::Departamentos de la UMU::Medicina | es |
dc.date.accessioned | 2024-01-23T09:42:45Z | - |
dc.date.available | 2024-01-23T09:42:45Z | - |
dc.date.issued | 2004-06 | - |
dc.identifier.citation | Journal of Bioenergetics and Biomembranes. 2004 Jun;36(3):265-73.doi: 10.1023/b:jobb.0000031978.15139.49. | es |
dc.identifier.issn | 1573-6881 | - |
dc.identifier.issn | 0145-479X | - |
dc.identifier.uri | http://hdl.handle.net/10201/137585 | - |
dc.description | ©2004. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/ This document is the Accepted version of a Published Work that appeared in final form in Journal of Bioenergetics and Biomembranes. To access the final edited and published work see https://doi.org/10.1023/b:jobb.0000031978.15139.49 | es |
dc.description.abstract | Isolated sarcoplasmic reticulum vesicles in the presence of Mg(2+) and absence of Ca(2+) retain significant ATP hydrolytic activity that can be attributed to the Ca(2+)-ATPase protein. At neutral pH and the presence of 5 mM Mg(2+), the dependence of the hydrolysis rate on a linear ATP concentration scale can be fitted by a single hyperbolic function. MgATP hydrolysis is inhibited by either free Mg(2+) or free ATP. The rate of ATP hydrolysis is not perturbed by vanadate, whereas the rate of p-nitrophenyl phosphate hydrolysis is not altered by a nonhydrolyzable ATP analog. ATP binding affinity at neutral pH and in a Ca(2+)-free medium is increased by Mg(2+) but decreased by vanadate when Mg(2+) is present. It is suggested that MgATP hydrolysis in the absence of Ca(2+) requires some optimal adjustment of the enzyme cytoplasmic domains. The Ca(2+)-independent activity is operative at basal levels of cytoplasmic Ca(2+) or when the Ca(2+) binding transition is impeded. | es |
dc.format | application/pdf | es |
dc.format.extent | 9 | es |
dc.language | eng | es |
dc.relation | This study was funded by grants BMC2002-02474 from Spanish Ministerio de Ciencia y Tecnologia/Fondo Europeo de Desarrollo Regional and PI-22/00756/FS/01 from Fundaci´on S´eneca de la Comunidad Aut´onoma de Murcia, Spain | es |
dc.rights | info:eu-repo/semantics/openAccess | es |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Ca2+-independent ATPase activity | es |
dc.subject | Ca2+-ATPase mechanism | es |
dc.subject | Sarcoplasmic reticulum Ca2+- ATPase | es |
dc.subject | Muscle relaxation | es |
dc.subject | Rabbit skeletal muscle | es |
dc.title | Functional approach to the catalytic site of the sarcoplasmic reticulum Ca(2+)-ATPase: binding and hydrolysis of ATP in the absence of Ca(2+) | es |
dc.type | info:eu-repo/semantics/article | es |
dc.identifier.doi | 10.1023/b:jobb.0000031978.15139.49 | - |
Aparece en las colecciones: | Artículos: Medicina |
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Functional Approach to the Catalytic Site of the Sarcoplasmic Reticulum Ca2+-ATPase Binding and Hydrolysis of ATP in the Absence of C.pdf | 265,99 kB | Adobe PDF | ![]() Visualizar/Abrir |
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