Cargando…
Introducing Negatively Charged Residues on the Surface of Fetal Hemoglobin Improves Yields in Escherichia coli
Fetal hemoglobin (HbF) has been developed into an important alternative protein for oxygen therapeutics. Such applications require extensive amounts of proteins, which only can be achieved via recombinant means. However, the expression of vertebrate hemoglobins in heterologous hosts is far from triv...
Autores principales: | Kettisen, Karin, Bülow, Leif |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8450383/ https://www.ncbi.nlm.nih.gov/pubmed/34552916 http://dx.doi.org/10.3389/fbioe.2021.721794 |
Ejemplares similares
-
Rapid Separation of Human Hemoglobin on a Large Scale From Non-clarified Bacterial Cell Homogenates Using Molecularly Imprinted Composite Cryogels
por: Hajizadeh, Solmaz, et al.
Publicado: (2021) -
Site-Specific Introduction of Negative Charges on the Protein Surface for Improving Global Functions of Recombinant Fetal Hemoglobin
por: Kettisen, Karin, et al.
Publicado: (2021) -
Structural and oxidative investigation of a recombinant high-yielding fetal hemoglobin mutant
por: Kettisen, Karin, et al.
Publicado: (2023) -
Site-directed mutagenesis of cysteine residues alters oxidative stability of fetal hemoglobin()
por: Kettisen, Karin, et al.
Publicado: (2018) -
Fetal hemoglobin is much less prone to DNA cleavage compared to the adult protein
por: Chakane, Sandeep, et al.
Publicado: (2017)