Cargando…
Rec. ST6Gal-I variants to control enzymatic activity in processes of in vitro glycoengineering
Autores principales: | Engel, Alfred M, Sobek, Harald, Greif, Michael, Malik, Sebastian, Thomann, Marco, Jung, Christine, Reusch, Dietmar, Ribitsch, Doris, Zitzenbacher, Sabine, Luley, Christiane, Schmoelzer, Katharina, Czabany, Tibor, Nidetzky, Bernd, Schwab, Helmut, Mueller, Rainer |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3980377/ http://dx.doi.org/10.1186/1753-6561-7-S6-P110 |
Ejemplares similares
-
High-quality production of human α-2,6-sialyltransferase in Pichia pastoris requires control over N-terminal truncations by host-inherent protease activities
por: Ribitsch, Doris, et al.
Publicado: (2014) -
In Vitro Glycoengineering of IgG1 and Its Effect on Fc Receptor Binding and ADCC Activity
por: Thomann, Marco, et al.
Publicado: (2015) -
Interaction analysis of glycoengineered antibodies with CD16a: a native mass spectrometry approach
por: Hajduk, Joanna, et al.
Publicado: (2020) -
Glycoform-resolved pharmacokinetic studies in a rat model employing glycoengineered variants of a therapeutic monoclonal antibody
por: Falck, David, et al.
Publicado: (2020) -
Polyol Structure and Ionic Moieties Influence the Hydrolytic Stability and Enzymatic Hydrolysis of Bio-Based 2,5-Furandicarboxylic Acid (FDCA) Copolyesters
por: Haernvall, Karolina, et al.
Publicado: (2017)