The substrate specificity of the magnesium-activated adenosinetriphosphatase of muscle
| ISSN: |
0003-9861
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|---|---|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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| Topics: |
Biology
Chemistry and Pharmacology
Physics
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| Type of Medium: |
Electronic Resource
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| URL: |
| _version_ | 1798292183023878144 |
|---|---|
| autor | Goldberg, M. Gilmour, D. |
| autorsonst | Goldberg, M. Gilmour, D. |
| book_url | http://dx.doi.org/10.1016/0003-9861(54)90496-8 |
| datenlieferant | nat_lic_papers |
| fussnote | The Mg-activated ATPase of muscle, first described by Kielley and Meyerhof, was found to split two phosphate groups from both ATP and ITP. The order of activity against the substrates was ATP 〉 ITP IDP 〉 ADP. Other organic phosphates and pyrophosphates were not attacked.The addition of alternative substrates caused an alteration (usually a decrease) in the rate of evolution of orthophosphate from both ATP and ITP, but the evidence did not conform with the requirements for competitive inhibition between the substrates.A number of inhibitors were found to affect the activity of the enzyme against both ATP and ITP.It was concluded that the substrate specificity of the ATPase was not restricted to the triphosphate grouping. |
| hauptsatz | hsatz_simple |
| identnr | NLZ183910311 |
| issn | 0003-9861 |
| journal_name | Archives of Biochemistry and Biophysics |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 51 (1954), S. 411-418 |
| search_space | articles |
| shingle_author_1 | Goldberg, M. Gilmour, D. |
| shingle_author_2 | Goldberg, M. Gilmour, D. |
| shingle_author_3 | Goldberg, M. Gilmour, D. |
| shingle_author_4 | Goldberg, M. Gilmour, D. |
| shingle_catch_all_1 | Goldberg, M. Gilmour, D. The substrate specificity of the magnesium-activated adenosinetriphosphatase of muscle 0003-9861 00039861 Elsevier |
| shingle_catch_all_2 | Goldberg, M. Gilmour, D. The substrate specificity of the magnesium-activated adenosinetriphosphatase of muscle 0003-9861 00039861 Elsevier |
| shingle_catch_all_3 | Goldberg, M. Gilmour, D. The substrate specificity of the magnesium-activated adenosinetriphosphatase of muscle 0003-9861 00039861 Elsevier |
| shingle_catch_all_4 | Goldberg, M. Gilmour, D. The substrate specificity of the magnesium-activated adenosinetriphosphatase of muscle 0003-9861 00039861 Elsevier |
| shingle_title_1 | The substrate specificity of the magnesium-activated adenosinetriphosphatase of muscle |
| shingle_title_2 | The substrate specificity of the magnesium-activated adenosinetriphosphatase of muscle |
| shingle_title_3 | The substrate specificity of the magnesium-activated adenosinetriphosphatase of muscle |
| shingle_title_4 | The substrate specificity of the magnesium-activated adenosinetriphosphatase of muscle |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:44:28.011Z |
| titel | The substrate specificity of the magnesium-activated adenosinetriphosphatase of muscle |
| titel_suche | The substrate specificity of the magnesium-activated adenosinetriphosphatase of muscle The Mg-activated ATPase of muscle, first described by Kielley and Meyerhof, was found to split two phosphate groups from both ATP and ITP. The order of activity against the substrates was ATP 〉 ITP IDP 〉 ADP. Other organic phosphates and pyrophosphates were not attacked.The addition of alternative substrates caused an alteration (usually a decrease) in the rate of evolution of orthophosphate from both ATP and ITP, but the evidence did not conform with the requirements for competitive inhibition between the substrates.A number of inhibitors were found to affect the activity of the enzyme against both ATP and ITP.It was concluded that the substrate specificity of the ATPase was not restricted to the triphosphate grouping. |
| topic | W V U |
| uid | nat_lic_papers_NLZ183910311 |