An improved method for the purification of IgG monoclonal antibodies from culture supernatants

D. A. Brooks, T. M. Bradford, J. J. Hopwood

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

A method for the purification of mouse monoclonal antibodies from hybridoma culture supernatants is described. The protocol involves the use of a combination of three previously described methods for the concentration and purification of monoclonal antibodies. Firstly, hybridomas were grown in a Diacult dialysis system (Inter Med Laboratory, Denmark) to yield milligram quantities of monoclonal antibody in a culture supernatant. Monoclonal antibodies were then purified from the culture supernatant by precipitation with polyethylene glycol 6000 (PEG 6000) and finally reprecipitated using an ammonium sulphate procedure. The PEG 6000 treatment caused a density change in the ammonium sulphate immunoglobulin precipitate, and resulted in the formation of a pellicle which contained pure mouse monoclonal antibody. The protocol removed contaminating bovine serum immunoglobulin as well as other serum and cellular protein from the monoclonal antibody preparations.

LanguageEnglish
Pages129-132
Number of pages4
JournalJournal of Immunological Methods
Volume155
Issue number1
DOIs
Publication statusPublished - 19 Oct 1992

Keywords

  • ELISA
  • Monoclonal antibody
  • Protein purification
  • Quantitationn

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Cite this

Brooks, D. A. ; Bradford, T. M. ; Hopwood, J. J. / An improved method for the purification of IgG monoclonal antibodies from culture supernatants. In: Journal of Immunological Methods. 1992 ; Vol. 155, No. 1. pp. 129-132.
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An improved method for the purification of IgG monoclonal antibodies from culture supernatants. / Brooks, D. A.; Bradford, T. M.; Hopwood, J. J.

In: Journal of Immunological Methods, Vol. 155, No. 1, 19.10.1992, p. 129-132.

Research output: Contribution to journalArticle

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