[go: up one dir, main page]

Lee et al., 2017 - Google Patents

Understanding of decreased sialylation of Fc‐fusion protein in hyperosmotic recombinant Chinese hamster ovary cell culture: N‐glycosylation gene expression and N …

Lee et al., 2017

View DOC
Document ID
15345079320082434920
Author
Lee J
Jeong Y
Kim Y
Lee G
Publication year
Publication venue
Biotechnology and Bioengineering

External Links

Snippet

To understand the effects of hyperosmolality on protein glycosylation, recombinant Chinese hamster ovary (rCHO) cells producing the Fc‐fusion protein were cultivated in hyperosmolar medium resulting from adding NaCl (415 mOsm/kg). The hyperosmotic culture showed …
Continue reading at www.researchgate.net (DOC) (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12PFERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00Preparation of peptides or proteins
    • C12P21/005Glycopeptides, glycoproteins
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/10Transferases (2.)
    • C12N9/1048Glycosyltransferases (2.4)
    • C12N9/1051Hexosyltransferases (2.4.1)
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6803General methods of protein analysis not limited to specific proteins or families of proteins
    • G01N33/6842Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle proteins
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/5005Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09Recombinant DNA-technology
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12PFERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00Preparation of peptides or proteins
    • C12P21/02Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/90Enzymes; Proenzymes

Similar Documents

Publication Publication Date Title
Lee et al. Understanding of decreased sialylation of Fc‐fusion protein in hyperosmotic recombinant Chinese hamster ovary cell culture: N‐glycosylation gene expression and N‐linked glycan antennary profile
Yin et al. Glycoengineering of Chinese hamster ovary cells for enhanced erythropoietin N‐glycan branching and sialylation
Tejwani et al. Glycoengineering in CHO cells: advances in systems biology
Lin et al. Chinese hamster ovary (CHO) host cell engineering to increase sialylation of recombinant therapeutic proteins by modulating sialyltransferase expression
Fan et al. Amino acid and glucose metabolism in fed‐batch CHO cell culture affects antibody production and glycosylation
Wong et al. An investigation of intracellular glycosylation activities in CHO cells: effects of nucleotide sugar precursor feeding
Morelle et al. Galactose supplementation in patients with TMEM165-CDG rescues the glycosylation defects
Castilho et al. In planta protein sialylation through overexpression of the respective mammalian pathway
Yamaji et al. A CRISPR screen using subtilase cytotoxin identifies SLC39A9 as a glycan-regulating factor
Yuk et al. Controlling glycation of recombinant antibody in fed‐batch cell cultures
US20120329709A1 (en) Production of glycoproteins
García-García et al. FUT8-directed core fucosylation of N-glycans is regulated by the glycan structure and protein environment
Fan et al. A multi‐pronged investigation into the effect of glucose starvation and culture duration on fed‐batch CHO cell culture
Bailey et al. Analysis of congenital disorder of glycosylation-Id in a yeast model system shows diverse site-specific under-glycosylation of glycoproteins
Maratha et al. Classical galactosaemia: novel insights in IgG N-glycosylation and N-glycan biosynthesis
MX2012011648A (en) High mannose glycans.
Hanzawa et al. Structures and developmental alterations of N-glycans of zebrafish embryos
Choi et al. N-glycan remodeling using mannosidase inhibitors to increase high-mannose glycans on acid α-glucosidase in transgenic rice cell cultures
Szulc et al. Biosynthesis of GlcNAc-rich N-and O-glycans in the Golgi apparatus does not require the nucleotide sugar transporter SLC35A3
Amann et al. CRISPR/Cas9‐multiplexed editing of Chinese hamster ovary B4Gal‐T1, 2, 3, and 4 Tailors N‐glycan profiles of therapeutics and secreted host cell proteins
Yin et al. A novel sugar analog enhances sialic acid production and biotherapeutic sialylation in CHO cells
Pandhal et al. Inverse metabolic engineering to improve Escherichia coli as an N‐glycosylation host
Valliere-Douglass et al. Asparagine-linked oligosaccharides present on a non-consensus amino acid sequence in the CH1 domain of human antibodies
Kajiura et al. Sialylation potentials of the silkworm, Bombyx mori; B. mori possesses an active α2, 6-sialyltransferase
Paschinger et al. The N-glycans of Trichomonas vaginalis contain variable core and antennal modifications