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Phosphate Binding in the Active Site of Alkaline Phosphatase and the Interactions of 2-Nitrosoacetophenone with Alkaline Phosphatase-Induced Small Structural Changes
To monitor structural changes during the binding of Pi to the active site of mammalian alkaline phosphatase in water medium, reaction-induced infrared spectroscopy was used. The interaction of Pi with alkaline phosphatase was triggered by a photorelease of ATP from the inactive P(3)-[1-(2-nitropheny...
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| Autori principali: | , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Biophysical Society
2004
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1304289/ https://ncbi.nlm.nih.gov/pubmed/15189884 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.103.034116 |
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