Thirty-five hybridomas that secrete mouse monoclonal antibodies (MAb)
against guinea pig (G.P.) tracheal mucins were established. The MAbs w
ere characterized immunologically, biochemically, and immunohistochemi
cally at both light and electron microscopic levels. Isotyping of the
MAbs revealed 14 to be IgM, 13 IgG(1), 3 IgG(2), and 5 IgG(3). The MAb
s demonstrated various patterns of binding in immunoblots against muci
ns 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 ind
icated that 33 of the 35 MAbs recognized carbohydrate epitopes on the
mucin molecules. Ten of the MAbs also reacted with both bovine and fer
ret tracheal mucins, while 7 and 6 MAbs bound only to bovine and ferre
t tracheal mucins, respectively. The generated MAbs should be useful f
or immunomeasurement of mucin secretion in vivo (e.g., in bronchoalveo
lar or airway lavage fluid) and in vitro (e.g., cell and organ culture
s) from cells of guinea pig and (with certain MAbs) bovine and ferret
origin.