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• W1975687798 startingPage "453" @default.
• W1975687798 abstract "The first full length IgG produced in Pichia pastoris was reported in late 1980. However, use of a wild-type Pichia expression system to produce IgGs with human-like N-linked glycans was not possible until recently. Advances in glycoengineering have enabled organisms such as Pichia to mimic human N-glycan biosynthesis and produce IgGs with human glycans on an industrial scale. Since there are only a few reports of the analytical characterization of Pichia-produced IgG, we summarize the results known in this field, and provide additional characterization data generated in our laboratories. The data suggest that Pichia-produced IgG has the same stability as that produced in Chinese hamster ovary (CHO) cells. It has similar aggregation profiles, charge variant distribution and oxidation levels as those for a CHO IgG. It contains human N-linked glycans and O-linked single mannose. Because of the comparable biophysical and biochemical characteristics, glycoengineered Pichia pastoris is an attractive expression system for therapeutic IgG productions." @default.
• W1975687798 created "2016-06-24" @default.
• W1975687798 creator A5003642180 @default.
• W1975687798 creator A5009802003 @default.
• W1975687798 creator A5045465134 @default.
• W1975687798 date "2011-09-01" @default.
• W1975687798 modified "2023-10-17" @default.
• W1975687798 title "Biochemical and biophysical characterization of humanized IgG1 produced in<i>Pichia pastoris</i>" @default.
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• W1975687798 doi "https://doi.org/10.4161/mabs.3.5.16891" @default.
• W1975687798 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3225849" @default.
• W1975687798 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22048694" @default.
• W1975687798 hasPublicationYear "2011" @default.
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