Cross-reactions among carbonic anhydrases I,II, and III studied by binding tests and with monoclonal antibodies |
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Authors: | Robert P Erickson Gary Kay David Hewett-Emmett Richard E Tashian J Latham Claflin |
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Institution: | (1) Department of Human Genetics, University of Michigan Medical School, 48109 Ann Arbor, Michigan;(2) Department of Microbiology and Immunology, University of Michigan Medical School, 48109 Ann Arbor, Michigan |
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Abstract: | Cross-reactions among carbonic anhydrases (CAs) I, II, and III were studied using a variety of antisera: (1) a rabbit antiserum to bovine CA III, (2) mouse antisera to human CA I, CA II, and CA III; and (3) five monoclonal antibodies prepared by the hybridoma technique using splenocytes from a mouse immunized with human CAs I and II and bovine CA III. Cross-reactions between CAs were readily found by binding assays using these antisera. Human CA I, but not human CA II, inhibited the reaction of the rabbit anti-CA III with its homologous antigen. Mouse antisera to CA I or CA II bound the homologous I or II with nearly as great efficiency as the autologous isozyme and sometimes weakly bound CA III. Mouse antisera to CA III frequently bound CA I or II. These cross-reactions were confirmed by the first use of hybridoma-prepared, monoclonal antibodies to CAs. The mouse monoclonal antibodies to CA isozymes varied in the amount of cross-reactivity among I, II, and III: at one extreme, one monoclonal was highly specific for the autologous CA III; at the other extreme, one monoclonal weakly reacted with some examples of CAs I, II, and III.This work was supported by NIH Grant GM-24681 and a grant from the National Foundation-March of Dimes. |
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Keywords: | carbonic anhydrase isozymes immunological cross-reactions monoclonal antibodies protein evolution |
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