Isolation and characterization of tracheobronchial mucin from a laryngectomee.
A tracheobronchial mucin was isolated from the tracheobronchial secretion of a laryngectomee. It was purified by gel filtration on Sepharose CL-6B in Tris-urea buffer and rechromatography of excluded materials through the same gel matrix. It was homogeneous in 0.7% agarose-2% polyacrylamide electrophoresis under nonreducing conditions. Comparable analysis with 2-mercaptoethanol revealed at least 3 subunits. Based upon recoverable weight, the mucin was composed of 75% carbohydrate, 21% protein, and 3% sulfate. Oligosaccharides obtained by alkaline beta-elimination indicated O-glycosyl linkage to the peptide component. Marked heterogeneity of the carbohydrate side-chains was reflected in the preparation of 20 distinct oligosaccharides ranging in size from 4 to 17 residues.
D000368:Aged; D000596:Amino Acids / Q000032:analysis; D001980:Bronchi / Q000378:metabolism*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007825:Laryngectomy; D046911:Macromolecular Substances; D008297:Male; D009077:Mucins / Q000302:isolation & purification*; D009844:Oligosaccharides / Q000032:analysis; D014132:Trachea / Q000378:metabolism*
D000596:Amino Acids; D046911:Macromolecular Substances; D009077:Mucins; D009844:Oligosaccharides