PHYSICAL PROPERTIES OF TAMM-HORSFALL GLYCOPROTEIN AND ITS GLYCOPOLYPEPTIDE
- 12 January 2009
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 10 (4) , 270-276
- https://doi.org/10.1111/j.1399-3011.1977.tb02797.x
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.Keywords
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