Recombinant human interferon-gamma. Differences in glycosylation and proteolytic processing lead to heterogeneity in batch culture.
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NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharidesHuman Mig chemokine: biochemical and functional characterizationHigh-level stable expression of recombinant 5-HT1A 5-hydroxytryptamine receptors in Chinese hamster ovary cellsN-glycosylation of recombinant human interferon-gamma produced in different animal expression systems.Effects of buffering conditions and culture pH on production rates and glycosylation of clinical phase I anti-melanoma mouse IgG3 monoclonal antibody R24.Glycan engineering of proteins with whole living yeast cells expressing rat liver alpha2,3-sialytransferase in the porous cell wall.Temperature reduction in cultures of hGM-CSF-expressing CHO cells: effect on productivity and product quality.N-glycans of recombinant human interferon-gamma change during batch culture of chinese hamster ovary cells.The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein.The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency.Animal cell cultures: recent achievements and perspectives in the production of biopharmaceuticals.Posttranslational processing of recombinant human interferon-gamma in animal expression systems.Monitoring proteolysis of recombinant human interferon-gamma during batch culture of Chinese hamster ovary cells.Optimisation of the cellular metabolism of glycosylation for recombinant proteins produced by Mammalian cell systems.Technological progresses in monoclonal antibody production systems.Molecular organization of the interferon gamma-binding domain in heparan sulphate.Fluorophore-labeled carbohydrate analysis of immunoglobulin fusion proteins: Correlation of oligosaccharide content with in vivo clearance profile.Multiple cell culture factors can affect the glycosylation of Asn-184 in CHO-produced tissue-type plasminogen activator.Metabolic effects on recombinant interferon-gamma glycosylation in continuous culture of Chinese hamster ovary cells.Regulation of N-linked core glycosylation: use of a site-directed mutagenesis approach to identify Asn-Xaa-Ser/Thr sequons that are poor oligosaccharide acceptors.N-linked glycosylation of GP5 of porcine reproductive and respiratory syndrome virus is critically important for virus replication in vivo.Expression of recombinant human interferon-γ with antiviral activity in the bi-cistronic baculovirus-insect/larval system.Influence of intracellular nucleotide and nucleotide sugar contents on recombinant interferon-gamma glycosylation during batch and fed-batch cultures of CHO cells.Fortification of a protein-free cell culture medium with plant peptones improves cultivation and productivity of an interferon-gamma-producing CHO cell line.Low glucose depletes glycan precursors, reduces site occupancy and galactosylation of a monoclonal antibody in CHO cell culture.Tetracycline-controlled expression of glycosylated porcine interferon-gamma in mammalian cells.Relationship between recombinant activated protein C secretion rates and mRNA levels in baby hamster kidney cells.Effect of different cell culture conditions on the polypeptide integrity and N-glycosylation of a recombinant model glycoprotein.Heterogeneity within populations of recombinant Chinese hamster ovary cells expressing human interferon-gamma.Role of N-glycosylation in the synthesis, dimerization and secretion of human interferon-gamma.Characterization of a recombinant antibody produced in the course of a high yield fed-batch process.The effect of the dilution rate on CHO cell physiology and recombinant interferon-gamma production in glucose-limited chemostat culture.Glucose-limited chemostat culture of Chinese hamster ovary cells producing recombinant human interferon-gamma.Enhanced erythropoietin heterogeneity in a CHO culture is caused by proteolytic degradation and can be eliminated by a high glutamine levelDifferent culture methods lead to differences in glycosylation of a murine IgG monoclonal antibody.Building high affinity human antibodies by altering the glycosylation on the light chain variable region in N-acetylglucosamine-supplemented hybridoma culturesGlycosylation: An intrinsic sign of "danger"Cell-free synthesis of enzymically active tissue-type plasminogen activator. Protein folding determines the extent of N-linked glycosylation.Efficient synthesis of polypeptide-α-thioester by the method combining polypeptide expression and chemical activation for the semi-synthesis of interferon-γ having oligosaccharides.Animal Cell Expression Systems.
P2860
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P2860
Recombinant human interferon-gamma. Differences in glycosylation and proteolytic processing lead to heterogeneity in batch culture.
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
@zh
1990年论文
@zh-cn
name
Recombinant human interferon-g ...... eterogeneity in batch culture.
@en
type
label
Recombinant human interferon-g ...... eterogeneity in batch culture.
@en
prefLabel
Recombinant human interferon-g ...... eterogeneity in batch culture.
@en
P2093
P2860
P356
P1433
P1476
Recombinant human interferon-g ...... eterogeneity in batch culture.
@en
P2093
Curling EM
Strange PG
P2860
P304
P356
10.1042/BJ2720333
P407
P577
1990-12-01T00:00:00Z