High-level expression and deletion mutagenesis of human tryptophan hydroxylase.
Human tryptophan hydroxylase has been expressed as a soluble and active form in Escherichia coli by fusion with an affinity tag, maltose-binding protein. The fusion protein has been purified to near homogeneity by affinity chromatography on crosslinked amylose resin. The purified fusion protein has...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1994
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC44262/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8022832/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.91.14.6659 |
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