Structure of Canine Tracheobronchial Mucin Glycoprotein
Canine tracheal mucin glycoprotein was isolated from beagle dogs fitted with tracheal pouches. Following exclusion chromatography on Sepharose CL-4B, noncovalently associated proteins were further resolved by dissociative density gradient centrifugation in CsBr-guanidinium chloride, and the mucin was then extracted with chloroform-methanol. The delipidated high-density product obtained had a nominal molecular weight of about 106 and an overall composition characteristic for a mucin glycoprotein, viz., a high content of serine and threonine, about 80% carbohydrate by weight, the absence of mannose or uronic acid, measurable ester sulfate, and a Pronase-resistant domain of molecular weight (1.75-3.0) X 105 which contains essentially all of the saccharide residues. Noncovalently bound lipid amounted to 6-10% by weight and was primarily cholesterol and cholesteryl esters. Cleavage of disulfide bonds by performic acid oxidation resulted in the release of a protein (Mr 65 000) not otherwise resolved by sodium dodecyl sulfate gel electrophoresis or the purification scheme. © 1987, American Chemical Society. All rights reserved.
Original Publication Date
DOI of published version
Woodward, Harold D.; Simet, Ira M.; Ringler, Nancy J.; Selvakumar, R.; Bhavanandan, V. P.; and Davidson, Eugene A., "Structure of Canine Tracheobronchial Mucin Glycoprotein" (1987). Faculty Publications. 4729.