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Monoclonal antibodies to glutathione S‐Transferase π–immunohistochemical analysis of human tissues and cancers
Author(s) -
Kantor Raphe R. S.,
Giardina Steven L.,
Bartolazzi Armando,
Townsend Allen J.,
Myers Charles E.,
Cowan Kenneth H.,
Longo Dan L.,
Natali Pier G.
Publication year - 1991
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910470206
Subject(s) - monoclonal antibody , polyclonal antibodies , immunohistochemistry , glutathione s transferase , microbiology and biotechnology , epitope , antibody , immunoassay , isozyme , glutathione , biology , monoclonal , enzyme , chemistry , biochemistry , immunology
Mouse monoclonal antibodies (MAb) have been generated against the anionic isozyme of human glutathione S‐transferase (GST π). MAb AGST I can inhibit 50‐70% of GST π enzymatic activity and reacts with a 3‐dimensional epitope which includes a putative glutathione binding site on GST π. A sandwich enzyme‐immunoassay established using MAb AGST I and a polyclonal antibody displayed a sensitivity of 0.5 ng/ml. Immunohistochemical analysis of human tissues demonstrated marked increases in GST π levels in cancers of the brain, cervix, endometrium, colon, rectum and testis and in fibro‐and chondrosarcomas.