Macromolecular architecture and hydrodynamic properties of human cervical mucins
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
Affiliations: [a] Department of Physiological Chemistry 2, University of Lund, P.O. Box 750, S-220 07 Lund, Sweden | [b] Department of Biological Sciences, University of Lancaster, Lancaster LA1 4YQ, U.K.
Abstract: Cervical mucus glycoproteins (mucins) were extracted by using slow stirring in 6M-guanidinium chloride supplemented with proteinase inhibitors. Subsequent purification was achieved by isopycnic density-gradient centrifugation in CsCl/guanidinium chloride. The whole mucins (Mr 10 × 106 – 15 × 106) were degraded into ‘subunits’ (Mr 2 × 106 – 3 × 106) by reduction. Trypsin digestion of subunits afforded glycopeptides (‘T-domains’) with Mr 0.4 × 106. The relationship between the intrinsic viscosity and Mr for the whole mucins and the fragments suggests that cervical mucins are linear flexible macromolecules. This view is supported by hydrodynamic data.
