Faculty Publications

Title

Structure of Canine Tracheobronchial Mucin Glycoprotein

Document Type

Article

Journal/Book/Conference Title

Biochemistry

Volume

26

Issue

17

First Page

5322

Last Page

5328

Abstract

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

1-1-1987

DOI of published version

10.1021/bi00391a016

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