Stabilities of antigen and antibody under elution conditions in immunoaffinity chromatography using monoclonal antibody.

Masamichi Kamihira, S. Iijima, T. Kobayashi

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

In immunoaffinity chromatography using monoclonal antibody, the elution conditions of an antigen, recombinant alpha-amylase, were studied. From among various conditions, three elution methods that gave fairly good yields of antigen activity (pH 2.3-2.5, pH 12.3-12.5 and 0.1 M lithium 3,5-diiodo salicylate [LIS]) were selected and the stabilities of the antigen and the antibody were analyzed. The antigen seemed to be eluted from the immunoadsorbent due to partial denaturation of either the antigen or the antibody. LIS seemed to be a specific denaturant for the antibody and its action was reversible. In terms of the stability of the antigen and repeated use of the immunoadsorbent, LIS seemed to be the best reagent for elution in immunoaffinity chromatography.

Original languageEnglish
Pages (from-to)185-188
Number of pages4
JournalBioseparation
Volume3
Issue number2-3
Publication statusPublished - Jan 1 1992
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Chemical Engineering(all)

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