Thirty-five hybridomas that secrete mouse monoclonal antibodies (MAb) against guinea pig (G.P.) tracheal mucins were established. The MAbs were characterized immunologically, biochemically, and immunohistochemically at both light and electron microscopic levels. Isotyping of the MAbs revealed 14 to be IgM, 13 IgG1, 3 IgG2, and 5 IgG3. The MAbs demonstrated various patterns of binding in immunoblots against mucins derived from G.P. tracheal explants. This suggested the presence of 'subpopulations' of G.P. tracheal mucins with specific MAbs binding to different epitopes on the mucin molecules. Periodate oxidation indicated that 33 of the 35 MAbs recognized carbohydrate epitopes on the mucin molecules. Ten of the MAbs also reacted with both bovine and ferret tracheal mucins, while 7 and 6 MAbs bound only to bovine and ferret tracheal mucins, respectively. The generated MAbs should be useful for immunomeasurement of mucin secretion in vivo (e.g., in bronchoalveolar or airway lavage fluid) and in vitro (e.g., cell and organ cultures) from cells of guinea pig and (with certain MAbs) bovine and ferret origin.
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