Microtiter radioimmunoprecipitation assay of HSV-1 polypeptides with recovery and SDS-PAGE analysis of precipatated proteins: Usefulness as screening test for large numbers of specimens including hybridoma supernates

Robert R. McKendall, Wayne Woo

Research output: Contribution to journalArticle

Abstract

Immunoprecipitation of radiolabeled polypeptides from complex mixtures of proteins was performed in polystyrene microtiter plates using staphylococcus protein A and various antibody preparations. The method is (1) rapid, (2) uses multichannel micropipettor technology, (3) handles large numbers of specimen easily, (4) requires very small volumes of antigen and antibody (5-50 μl), (5) provides replicates for statistical analysis and (6) allows recovery of precipitated proteins for direct SDS-PAGE analysis of precipitated proteins. We have shown it is useful as a test to screen large numbers of sera or to characterize monoclonal antibody-containing samples.

Original languageEnglish (US)
Pages (from-to)461-469
Number of pages9
JournalJournal of Immunological Methods
Volume72
Issue number2
DOIs
StatePublished - Sep 4 1984

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Radioimmunoprecipitation Assay
Hybridomas
Human Herpesvirus 1
Polyacrylamide Gel Electrophoresis
Peptides
Proteins
Antibodies
Polystyrenes
Staphylococcal Protein A
Complex Mixtures
Staphylococcus
Immunoprecipitation
Monoclonal Antibodies
Technology
Antigens
Serum

Keywords

  • HSV-1 polypeptides
  • hybridoma screening
  • microtiter radioimmunoprecipitation

ASJC Scopus subject areas

  • Biotechnology
  • Immunology

Cite this

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AU - Woo, Wayne

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AB - Immunoprecipitation of radiolabeled polypeptides from complex mixtures of proteins was performed in polystyrene microtiter plates using staphylococcus protein A and various antibody preparations. The method is (1) rapid, (2) uses multichannel micropipettor technology, (3) handles large numbers of specimen easily, (4) requires very small volumes of antigen and antibody (5-50 μl), (5) provides replicates for statistical analysis and (6) allows recovery of precipitated proteins for direct SDS-PAGE analysis of precipitated proteins. We have shown it is useful as a test to screen large numbers of sera or to characterize monoclonal antibody-containing samples.

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