کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
20481 43176 2014 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Glycosylation analysis of an aggregated antibody produced by Chinese hamster ovary cells in bioreactor culture
ترجمه فارسی عنوان
تجزیه و تحلیل گلیکوزیلیت یک آنتیبادی جمع آوری شده توسط سلول های تخمدان هامستر چینی در کشت بیوراکتور
کلمات کلیدی
سلول تخمدان هامستر چینی، فرهنگ سلولی، تولید آنتی بادی، تجمع آنتی بادی، ناهمگنی گلیکوزیلات، دیابت بیضوی
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
چکیده انگلیسی

N-Glycosylation of therapeutic antibodies contributes not only to their biological function, but also to their stability and tendency to aggregate. Here, we investigated the impact of the glycosylation status of an aggregated antibody that accumulated during the bioreactor culture of Chinese hamster ovary cells. High-performance liquid chromatography analysis showed that there was no apparent difference in the glycosylation patterns of monomeric, dimeric, and large aggregated forms of the antibody. In contrast, lectin binding assays, which enable the total amounts of specific sugar residues to be detected, showed that both galactose and fucose residues in dimers and large aggregates were reduced to 70–80% of the amount in monomers. These results strongly suggest that the lack of N-linked oligosaccharides, a result of deglycosylation or aglycosylation, occurred in a proportion of the dimeric and large aggregated components. The present study demonstrates that glycosylation heterogeneities are a potential cause of antibody aggregation in cell culture of Chinese hamster ovary cells, and that the lack of N-glycosylation promotes the formation of dimers and finally results in large aggregates.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Bioscience and Bioengineering - Volume 117, Issue 5, May 2014, Pages 639–644
نویسندگان
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