Novel purification method of human immunoglobulin by using a thermo-responsive protein A

Ichiro Koguma, Shuntaro Yamashita, Satoshi Sato, Kazuo Okuyama, Yoshinori Katakura

研究成果: Contribution to journalArticle

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We attempted to evaluate a novel purification method of immunoglobulins (IgGs) by using a mutant type of protein A. Although this mutant protein A binds to IgGs at 5 °C, the IgGs are released at 40 °C; hence, it was designated as thermo-responsive protein A (TRPA). We aimed to purify IgG1 from the culture supernatant of CHO cells producing AE6F4 human monoclonal IgG1. AE6F4 IgG1 was purified using only a TRPA-filled column and by modifying the temperature, without any exposure to acidic conditions. Furthermore, the purified AE6F4 IgG1 maintained the inherent binding affinity to antigen, while this property was lost in AE6F4 IgG1 purified using a conventional protein A (CPA) column possibly because of product aggregation and fragmentation. These data suggest that IgG is sensitive to acid treatment; however, it can be highly purified with retention of high affinity by using a TRPA column. Further, this purification method can be used on an industrial scale for the purification of antibody drugs.

元の言語英語
ページ(範囲)149-153
ページ数5
ジャーナルJournal of Chromatography A
1305
DOI
出版物ステータス出版済み - 8 30 2013

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry

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