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

Erik A.C. Wiemer; Rob Ofman; Esther Middelkoop; Mark de Boer; Ronald J.A. Wanders; Joseph M. Tager

doi:10.1016/0022-1759(92)90115-A

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

Erik A.C. Wiemer
, Rob Ofman
, Esther Middelkoop^*
, Mark de Boer
, Ronald J.A. Wanders
, Joseph M. Tager

^*Corresponding author for this work

University of Amsterdam
N.V. Innogenetics

Research output: Contribution to journal › Article › Academic › peer-review

18 Citations (Scopus)

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.

Original language	English
Pages (from-to)	165-175
Number of pages	11
Journal	Journal of Immunological Methods
Volume	151
Issue number	1-2
DOIs	https://doi.org/10.1016/0022-1759(92)90115-A
Publication status	Published - 6 Jul 1992
Externally published	Yes

Bibliographical note

The authors are grateful to Bram Bout, Stanley Brul and Tycho Schoenmaker for helpful discussions.

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10.1016/0022-1759(92)90115-A

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title = "Production and characterisation of monoclonal antibodies against native and disassembled human catalase",

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.",

author = "Wiemer, \{Erik A.C.\} and Rob Ofman and Esther Middelkoop and Boer, \{Mark de\} and Wanders, \{Ronald J.A.\} and Tager, \{Joseph M.\}",

note = "The authors are grateful to Bram Bout, Stanley Brul and Tycho Schoenmaker for helpful discussions.",

year = "1992",

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doi = "10.1016/0022-1759(92)90115-A",

language = "English",

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journal = "Journal of Immunological Methods",

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TY - JOUR

T1 - Production and characterisation of monoclonal antibodies against native and disassembled human catalase

AU - Wiemer, Erik A.C.

AU - Ofman, Rob

AU - Middelkoop, Esther

AU - Boer, Mark de

AU - Wanders, Ronald J.A.

AU - Tager, Joseph M.

N1 - The authors are grateful to Bram Bout, Stanley Brul and Tycho Schoenmaker for helpful discussions.

PY - 1992/7/6

Y1 - 1992/7/6

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0026635891

U2 - 10.1016/0022-1759(92)90115-A

DO - 10.1016/0022-1759(92)90115-A

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VL - 151

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EP - 175

JO - Journal of Immunological Methods

JF - Journal of Immunological Methods

IS - 1-2

ER -

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

Abstract

Bibliographical note

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