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Light scattering studies of proteoglycans

Zangrando, David Duane
http://rave.ohiolink.edu/etdc/view?acc_num=case1055947716

Abstract Details

1991, Doctor of Philosophy, Case Western Reserve University, Macromolecular Science.
Laser light scattering has been used to investigate the structure and hydrodynamic properties of proteoglycans. Two species of proteoglycans have been studied in this work. The first proteoglycan species is that isolated from bovine skin, and is called proteodermatan sulfate (PDS). The second proteoglycan species is isolated from bovine nasal septum cartilage, and exists in two forms: the subunit or monomeric form (PGS), and the aggregate form (PGA), in which PGS units are non-covalently attached to a linear strand of hyaluronic acid (HA). Static light scattering was used to determine the weight-average molecular weight, Mw, z-average radius of gyration, Rgz, and the second virial coefficient, A2. Dynamic light scattering was used to obtain the z-average translational diffusion coefficient, Dtz, which at infinite dilution allows the frictional hydrodynamic radius, Rhf, to be determined using the Stoke's equation. PDS was determined to have a Mw = 62,000 in 4M guanidine hydrochloride (GndHCl), which increased to 610,000 in 0.15M NaCl. The core protein was found to have a Mw = 39,000 in GndHCl, and this also significantly increased to 650,000 in 0.15M NaCl. In contrast, the dermatan sulfate chain (DS) was determined to have a Mw = 24,000 in 0.15M NaCl, indicating minimal self-association. Comparison of the observed translational diffusion coefficient with various hydrodynamic models indicates that PDS has a "lollipop" conformation in dilute solution. The Rgz for PDS (53 nm) and core protein (34 nm) are significantly above expected values for their respective molecular weights. This discrepancy is consistent with a small degree (<5%) of self-association of PDS and core protein in 4M GndHCl. The dilute solution hydrodynamic behavior of PGS and PGA were found to deviate from conventional hydrodynamic theory. Initially, experimental error in the light scattering results was suspected. However, upon further review of proteoglycan literature, as well as literature on star- and comb-branched polymers, it was noted that similar deviations from conventional theory also occurred. Following this observation, a review of more recent hydrodynamic theories was performed, which showed that branched molecular systems are not adequately explained by conventional theory. Finally, the thermal stability of both the PGS and link-stabilized PGA was evaluated. This represents the first time the thermal stability of the subunit was investigated.
John Blackwell (Advisor)
228 p.
Biology, Molecular
Light scattering; proteoglycans

Recommended Citations

Citations

  • Zangrando, D. D. (1991). Light scattering studies of proteoglycans [Doctoral dissertation, Case Western Reserve University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=case1055947716

    APA Style (7th edition)

  • Zangrando, David. Light scattering studies of proteoglycans. 1991. Case Western Reserve University, Doctoral dissertation. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=case1055947716.

    MLA Style (8th edition)

  • Zangrando, David. "Light scattering studies of proteoglycans." Doctoral dissertation, Case Western Reserve University, 1991. http://rave.ohiolink.edu/etdc/view?acc_num=case1055947716

    Chicago Manual of Style (17th edition)

case1055947716
512
© 1991, all rights reserved.
This open access ETD is published by Case Western Reserve University School of Graduate Studies and OhioLINK.