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| Format: | Artículo científico |
| Language: | en |
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Academia Brasileira de Ciências
2000
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| Online Access: | https://www.redalyc.org/articulo.oa?id=32772310 |
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| _version_ | 1866556804143513600 |
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| author | Leopoldo de Meis |
| author_facet | Leopoldo de Meis |
| contents | Energy Interconversion by the Sarcoplasmic Reticulum Ca2+-ATPase: ATP Hydrolysis, Ca2+ Transport, ATP Synthesis and Heat Production Leopoldo de Meis Multidisciplinaria (Ciencias Naturales y Exactas) Ca2+ ATPase Ca2+ transport ATP hydrolysis heat production The sarcoplasmic reticulum of skeletal muscle retains a membrane bound Ca2+-ATPase which is ableto interconvert different forms of energy. A part of the chemical energy released during ATP hydrolysis isconverted into heat and in the bibliography it is assumed that the amount of heat produced during the hydrolysisof an ATP molecule is always the same, as if the energy released during ATP cleavage were divided in twonon-interchangeable parts: one would be converted into heat, and the other used for Ca2+ transport. Dataobtained in our laboratory during the past three years indicate that the amount of heat released during thehydrolysis of ATP may vary between 7 and 32 Kcal/mol depending on whether or not a transmembraneCa2+ gradient is formed across the sarcoplasmic reticulum membrane. Drugs such as heparin and dimethylsulfoxide are able to modify the fraction of the chemical energy released during ATP hydrolysis which isused for Ca2+ transport and the fraction which is dissipated in the surrounding medium as heat. 2000 artículo científico 0001-3765 https://www.redalyc.org/articulo.oa?id=32772310 en http://www.redalyc.org/revista.oa?id=327 Anais da Academia Brasileira de Ciências application/pdf Academia Brasileira de Ciências Anais da Academia Brasileira de Ciências (Brasil) Num.3 Vol.72 |
| format | Artículo científico |
| id | redalyc_32772310 |
| language | en |
| publishDate | 2000 |
| publisher | Academia Brasileira de Ciências |
| spellingShingle | Energy Interconversion by the Sarcoplasmic Reticulum Ca2+-ATPase: ATP Hydrolysis, Ca2+ Transport, ATP Synthesis and Heat Production Leopoldo de Meis Multidisciplinaria (Ciencias Naturales y Exactas) Ca2+ ATPase Ca2+ transport ATP hydrolysis heat production Energy Interconversion by the Sarcoplasmic Reticulum Ca2+-ATPase: ATP Hydrolysis, Ca2+ Transport, ATP Synthesis and Heat Production Leopoldo de Meis Multidisciplinaria (Ciencias Naturales y Exactas) Ca2+ ATPase Ca2+ transport ATP hydrolysis heat production The sarcoplasmic reticulum of skeletal muscle retains a membrane bound Ca2+-ATPase which is ableto interconvert different forms of energy. A part of the chemical energy released during ATP hydrolysis isconverted into heat and in the bibliography it is assumed that the amount of heat produced during the hydrolysisof an ATP molecule is always the same, as if the energy released during ATP cleavage were divided in twonon-interchangeable parts: one would be converted into heat, and the other used for Ca2+ transport. Dataobtained in our laboratory during the past three years indicate that the amount of heat released during thehydrolysis of ATP may vary between 7 and 32 Kcal/mol depending on whether or not a transmembraneCa2+ gradient is formed across the sarcoplasmic reticulum membrane. Drugs such as heparin and dimethylsulfoxide are able to modify the fraction of the chemical energy released during ATP hydrolysis which isused for Ca2+ transport and the fraction which is dissipated in the surrounding medium as heat. 2000 artículo científico 0001-3765 https://www.redalyc.org/articulo.oa?id=32772310 en http://www.redalyc.org/revista.oa?id=327 Anais da Academia Brasileira de Ciências application/pdf Academia Brasileira de Ciências Anais da Academia Brasileira de Ciências (Brasil) Num.3 Vol.72 |
| title | Energy Interconversion by the Sarcoplasmic Reticulum Ca2+-ATPase: ATP Hydrolysis, Ca2+ Transport, ATP Synthesis and Heat Production |
| topic | Multidisciplinaria (Ciencias Naturales y Exactas) Ca2+ ATPase Ca2+ transport ATP hydrolysis heat production |
| url | https://www.redalyc.org/articulo.oa?id=32772310 |