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Kinetics of electron transfer in the complex of cytochrome P450 3A4 with the flavin domain of cytochrome P450BM-3 as evidence of functional heterogeneity of the heme protein
We used a rapid scanning stop-flow technique to study the kinetics of reduction of cytochrome P450 3A4 (CYP3A4) by the flavin domain of cytochrome P450-BM3 (BMR), which was shown to form a stoichiometric complex (K(D) = 0.48 µM) with CYP3A4. In the absence of substrates only about 50% of CYP3A4 was...
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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2007
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2346489/ https://ncbi.nlm.nih.gov/pubmed/18086551 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.abb.2007.11.020 |
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