A polydisperse linear random coil model for the quaternary structure of pig colonic mucin.

The distribution of molecular weights for polymeric colonic mucus glycoprotein or "mucin" isolated and solubilised in the presence of protease inhibitors from pig colons is shown to be considerably greater than its "subunit" (thiol reduction product) and papain digested forms using the technique of size-exclusion chromatography coupled to multi-angle laser light scattering, and confirmed by sedimentation equilibrium measurements. The conformation of this mucin is probed by examining the molecular weight-intrinsic viscosity relationship in terms of the Mark-Houwink-Kuhn-Sakurada analysis for its polymeric (or "whole"), reduced and papain-digested forms: an exponent "a" of (1.1 +/- 0.1) is obtained indicating a linear random coil conformation consistent with other mucins. Size-exclusion chromatography coupled to multi-angle laser light scattering is shown to provide a relatively simple complementary technique to sedimentation equilibrium for the molecular weight distribution analysis of polydisperse materials.