Production and characterization of monoclonal antibody to recombinantα-amylase

Masamichi Kamihira, Ichirou Kawakubo, Shinji Iijima, Masayuki Taniguchi

研究成果: ジャーナルへの寄稿記事

17 引用 (Scopus)

抜粋

Four hybridoma cell lines that secreted monoclonal antibodies against thermostable a-amylase produced by a recombinant Eseherichia coli were established. One of the clones, designated 16-3F, was quite stable with good growth in DF-ITES serum-free medium and high production of the antibody. Cell growth was independent of insulin, ethanolamine and selenite, but it strongly depended on transferrin. In the serum-free media the specific antibody production rate was almost constant irrespective of cell growth. Repeated batch culture in DF medium was found to be promising for antibody production after cell density was increased in DF-ITES medium. The affinity constant between the antibody and the antigen measured by a solid-phase ELISA was 1.3 x 108dm3/mol. The antibody did not bind four kinds of a-amylase derived from other organisms.

元の言語英語
ページ(範囲)357-362
ページ数6
ジャーナルJOURNAL OF CHEMICAL ENGINEERING OF JAPAN
21
発行部数4
DOI
出版物ステータス出版済み - 1 1 1988
外部発表Yes

    フィンガープリント

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)

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