Production and characterization of monoclonal antibody to recombinant .ALPHA.-amylase.

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概要

• 論文の詳細を見る

• Four hybridoma cell lines that secreted monoclonal antibodies against thermostable α-amylase produced by a recombinant Escherichia 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 × 108dm3/mol. The antibody did not bind four kinds of α-amylase derived from other organisms.

• 公益社団法人 化学工学会の論文

著者

• Kamihira Masamichi

  Department Of Biotechnology Graduate School Of Engineering Nagoya University

• Kobayashi Takeshi

  Department Of Biological Chemistry College Of Bioscience And Biotechnology Chubu University

• Taniguchi Masayuki

  Department Of Cardiology Jikei University School Of Medicine Daisan Hospital

• IIJIMA Shinji

  Department of Agricultural Chemistry, The University of Tokyo

• KAWAKUBO ICHIROU

  Department of Chemical Engineering, Nagoya University

• Kamihira Masamichi

  Department of Chemical Engineering, Nagoya University

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