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Issue title: Special Double Issue for the Fifth International Congress of Biorheology. Dedicated to Hellmut Hartert. Baden-Baden, F.R. Germany, 20–24 August 1983
Guest editors: Alfred L. Copley
Article type: Research Article
Authors: Steiner, C.A.a; * | Litt, M.a; b | Nossal, R.c
Affiliations: [a] Department of Chemical Engineering, University of Pennsylvania, Philadelphia, Pennsylvania | [b] Department of Bioengineering, University of Pennsylvania, Philadelphia, Pennsylvania | [c] National Institutes of Health, Bethesda, Maryland
Note: [*] Present address: Research Center, Hercules, Inc., Wilmington, Delaware
Abstract: Mucin glycoproteins are known to be the principal determinants of epithelial mucus rheology and hence of mucociliary transport rates. We are studying the structure of such glycoproteins using a model mucin purified from canine tracheal pouch secretions. Of particular interest is the effect on mucin structure of increased Ca++ such as occurs in certain disease states. Quasielastic laser light scattering was used to study the effect of Ca++ on the hydrodynamic radius of the mucin molecules. Scattering data from 0.3 mg/ml mucin solutions in physiological phosphate buffer containing 0,5 × 10−5 M, and 5 × 10−4 M Ca++ were analyzed to obtain an average translational diffusion coefficient and the distribution of molecular radii for the dispersion. The effect of Ca++ was to decrease the average Stokes radius. The light scattering results are supported by rheologic measures of mucin gel viscoelasticity.
Keywords: mucin, rheology, Ca++, tracheal mucus, macromolecular structure
DOI: 10.3233/BIR-1984-211-226
Journal: Biorheology, vol. 21, no. 1-2, pp. 235-252, 1984
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