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 fo
Small-Angle X-Ray Scattering on Solutions of Carboxymethylcellulose and Bovine Serum Albumin
β Scribed by Sabrina M. Pancera; Rosangela Itri; Denise F. S. Petri
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 137 KB
- Volume
- 5
- Category
- Article
- ISSN
- 1616-5187
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β¦ Synopsis
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·βmL^β1^ were investigated. Upturns in the very low q range revealed the presence of aggregates when the CMC concentration was higher than 2βΓβ10^β3^ gβΒ·βmL^β1^. The comparison between the calculated form factor with the experimental curves at intermediate and long q values indicated that the BSA molecules keep their native form in mixtures with CMC concentrations lower than 5βΓβ10^β3^ gβΒ·βmL^β1^. Therefore, for CMC concentrations higher than 2βΓβ10^β3^ gβΒ·βmL^β1^ the mixtures start to present aggregates and free BSA molecules coexisting in solution.
SAXS evidenced the complex formation between BSA and carboxymethylcellulose (CMC) at a stoichiometric ratio. Excess of CMC led to aggregation.
magnified imageSAXS evidenced the complex formation between BSA and carboxymethylcellulose (CMC) at a stoichiometric ratio. Excess of CMC led to aggregation.
π SIMILAR VOLUMES
Osmotic pressure measurements of human serum albumin (HSA) dissolved in water and in 0.01, 0.1, and 1.0 M phosphate buffer are reported as a function of the protein concentration. Two different forms of the protein were studied: defatted HSA (HSA1) and HSA with fatty acids (HSA2). The measured value
Smal I -a n g l e x -r a y s c a t t e r i n g (SAXRS) s t u d i e s o f t h e human serum h i g h -d e n s i t y l i p o p r o t e i n HDL2 i n d i c a t e a symmetrical p a r t i c l e w i t h a r a d i u s o f g y r a t i o n Rg = 46 A. t i e s o f s u b s i d i a r y maxima i n t h e s c a t t e
We investigated the structure of silk fibroin dissolved in water and in water-organic solvent mixtures by CD and small-angle x-ray scattering (SAXS). CD spectra indicated a disordered secondary structure in water and a 8-sheet conformation in aqueous organic solvents, such as methanol, dioxane, and
The polymerization of macromonomers provides polymers of extremely high branching density with regular branch length, branching number and branching interval. The intrinsic shape and size of these polymacromonomers were evaluated by small-angle X-ray scattering. The conformation of the backbone and
## Abstract The crossβsectional radius of gyration of the deoxyribonucleoprotein (DNP) threads was measured by smallβangle Xβray scattering in a wide range of ionic strengths (from 0.0005 to 2 __M__ NaCl). For DNP in a solution of low ionic strength, this value is 30 Γ . The increase of ionic streng