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Quantification of residual hydrophobic fusion peptide with monomer and dimer forms using reversed-phase liquid chromatography
A fusion peptide mimicking a part of the sequence of HIV-1 envelope glycoprotein with an additional cysteine at its C-terminus (FP8: AVGIGAVFC) was conjugated to a carrier protein through a linker for development of an HIV-1 vaccine. Since this fusion peptide is very hydrophobic with poor solubility...
Tallennettuna:
| Julkaisussa: | J Chromatogr B Analyt Technol Biomed Life Sci |
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| Päätekijät: | , , , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2020
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC8138758/ https://ncbi.nlm.nih.gov/pubmed/32224438 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jchromb.2020.122073 |
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