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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.
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