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

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Abstract
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.

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