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Electrostatic compared with hydrophobic interactions between bovine serum amine oxidase and its substrates.
A steady-state kinetic study of bovine serum amine oxidase activity was performed, over a wide range of pH values (5.4-10.2) and ionic strength (10-200 mM), using various (physiological and analogue) substrates as specific probes of the active-site binding region. Relatively small changes in k (cat)...
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| Główni autorzy: | , , , , , , |
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| Format: | Artigo |
| Język: | Inglês |
| Wydane: |
2003
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| Hasła przedmiotowe: | |
| Dostęp online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1223303/ https://ncbi.nlm.nih.gov/pubmed/12529179 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20021055 |
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