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Multiple apomucin translation products from human respiratory mucosa mRNA.

European journal of biochemistry / FEBS

metabolism, Animals, Antibodies, Monoclonal, diagnostic use, Antibody Specificity, Blotting, Northern, DNA, genetics, DNA Probes, Electrophoresis, Polyacrylamide Gel, Epitopes, Gastric Mucins, Humans, Male, Mice, Mice, Inbred BALB C, Mucins, Mucous Membrane, Nucleic Acid Hybridization, Peptides, Precipitin Tests, Protein Biosynthesis, Protein Precursors, RNA, Messenger, isolation & purification, Respiratory System

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      Poly(A)-rich RNA was purified from a pool of five human tracheobronchial mucosa. After in vitro translation in a reticulocyte lysate and immunoprecipitation of the translated products, using either a polyclonal antiserum or a monoclonal antibody to deglycosylated respiratory mucin peptides, the products were characterized by SDS/PAGE. The respiratory mucin precursors migrated as a very large smear from almost the top of the resolving polyacrylamide gel to an area corresponding to a molecular mass of about 100 kDa. After hybridization with mucin cDNA probe TH 29 described by Crepin et al. [Crepin, M., Porchet, N., Aubert, J. P. & Degand, P. (1990) Biorheology 27, 471-484] respiratory mucin mRNAs also appeared polydisperse. Although degradation or incomplete translation of high-molecular-mass mRNA cannot be entirely ruled out, these results suggest that human respiratory apomucins consist of a family of peptides which share some common epitopes. This possibility is in agreement with (a) the diversity of mucin precursors observed previously with pulse/chase experiments performed with explants of human respiratory mucosa and (b) the polydispersity of secreted respiratory mucins observed by electron microscopy.

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