PHYSICAL PROPERTIES OF TAMM-HORSFALL GLYCOPROTEIN AND ITS GLYCOPOLYPEPTIDE

Abstract
The MW of the constituent glycopolypeptide chain of Tamm-Horsfall (T-H) glycoprotein [human] was determined by sedimentation equilibrium under 2 entirely different sets of denaturing conditions. For both sets of denaturing conditions the average MW estimated for T-H glycopolypeptide was 74,000. The gel chromatographic behavior in 6 M guanidium chloride of T-H glycopolypeptide with disulfide bonds intact as compared with its gel chromatographic behavior with disulfide bonds broken indicated that the glycopolypeptide is highly constrained by intrachain disulfide bonds.