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Production and characterisation of monoclonal antibodies against native and disassembled human catalase

Authors
Publisher
Elsevier B.V.
Publication Date
Volume
151
Identifiers
DOI: 10.1016/0022-1759(92)90115-a
Keywords
  • Catalase
  • Monoclonal Antibody
  • Peroxisome
  • Peroxisomal Biogenesis
Disciplines
  • Biology

Abstract

Abstract Catalase isolated from human erythrocytes was used to immunise mice, in order to generate hybridomas producing specific monoclonal antibodies to the enzyme. Hybridomas secreting anti-(catalase) antibodies were identified by a modified enzyme-linked immunosorbent assay (ELISA) using either monomer/dimer catalase or native, tetrameric enzyme. Three stable hybridomaclones were selected and the characteristics of the antibodies produced were investigated by ELISA, immunofluorescence, immunoprecipitation and immunoblotting experiments. One monoclonal antibody (17E10) was shown to interact with both native tetramer catalase and - to a lesser extent - withmonomer/dimer catalase. Two monoclonal antibodies (10B12H9, 13A10) were found to react only with completely denatured catalase or with monomer/dimer catalase but not with native catalase.

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