Light scattering studies of bovine skin proteodermatan sulfate

✍ Scribed by David Zangrando; Rekha Gupta; Alex M. Jamieson; John Blackwell; Paul G. Scott

• Publisher: Wiley (John Wiley & Sons)
• Year: 1989
• Tongue: English
• Weight: 792 KB
• Volume: 28
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360280710

✦ Synopsis

The proteodermatan sulfate (PDS) of bovine skin is a low molecular weight proteoglycan with a molecular structure consisting of a protein chain and a sulfated polysaccharide chain covalently linked at the 4-serine of the protein. Static and dynamic laser light scattering methods have been used to determine the weight-average molecular weight, M,, z-average radius of gyration, Rg,, and z-average translational diffusion coe5cient, DC,, of bovine skin PDS. We have also characterized the two components of PDS, i.e., the protein core and the dermatan sulfate (DS) chain. (The latter contained an N-terminal-linked penta-or tetrapeptide.) Interpretation of the PDS data is complicated by the block copolymer nature of its structure. When appropriate corrections are made, our results indicate that M, for PDS monomer is 62,000 when dissolved in 4M guanidine hydrochloride (GdnHCl), and increases to 610,000 in 0.15M NaCl. M, for the core protein in 4M GdnHCl is 39,000, and this also increases substantially to 650,000 in 0.15M NaC1. In contrast, M, for the DS chain is 24,000 in 0.15M NaCl, indicating that there is minimal self-association of DS in 0.15M NaCl. Thus we conclude that the self-association of PDS involves the protein core. Comparison of Rgz and R,, the average hydrodynamic radius, suggests that trace amounts of aggregation persist for the PDS and its core protein even in 4M GdnHCl. This conclusion is supported by evaluation of the second moments of the dynamic light scattering correlation function. Comparisons of the observed DZz for PDS with predicted values using hydrodynamic theory are consistent with a "lollipop" conformation for the molecule.