## Abstract **Summary:** The existence of attractive interaction between CMC and BSA was evidenced in solution at pH higher than the protein isoelectric point by means of SAXS. Mixtures of BSA at 10βΓβ10^β3^ gβΒ·βmL^β1^ and CMC at the concentration range of 1βΓβ10^β3^ gβΒ·βmL^β1^ to 10βΓβ10^β3^ gβΒ·βm
Small-angle x-ray scattering of bovine nasal cartilage proteoglycan in solution
β Scribed by S. S. Stivala; A. Patel; B. Khorramian; J. D. Gregory; S. Damle
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1987
- Tongue
- English
- Weight
- 954 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
The proteoglycan subunit (PGS) from bovine nasal cartilage was examined in water and in 0.15 N LiCl by small-angle x-ray scattering (SAXS). The molecular weight of 2.5 X lo6 and the radius of gyration, R, = 493 in 0.15 N LiC1, obtained by SAXS, are in good agreement with values reported by others for similar preparations. Values of the radius of gyration of the cross section, mass per unit length, and persistence length of the PGS are also reported. The low value of intrinsic viscosity ([q]) found in 0.15 N LiC1, and a comparison of the experimental distance distribution function to that of the theoretical distance distribution function for sphere, suggest that the FGS in salt solution approaches spherical symmetry. The much higher value of [q] in water suggests a prolate ellipsoid of low axial ratio.
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