Macromolecular architecture and hydrodynamic properties of human cervical mucins.
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 X 10(6) - 15 X 10(6)) were degraded into subunits (Mr 2 X 10(6) - 3 X 10(6)) by reduction. Trypsin digestion of subunits afforded glycopeptides (T-domains) with Mr 0.4 X 10(6). 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.
D002582:Cervix Mucus / Q000032:analysis*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D005260:Female; D006801:Humans; D046911:Macromolecular Substances; D009077:Mucins / Q000302:isolation & purification* / Q000502:physiology
D046911:Macromolecular Substances; D009077:Mucins