Serum albumin hydrodynamic properties

Monkos, Karol 2005. A comparison of solution conformation and hydrodynamic properties of equine, porcine and rabbit serum albumin using viscometric measurements. Biochimica et Biophysica Acta 1748,100-109. 

Often utilized as a substitute for a typical protein, albumin needs no introduction to the protein chemist. Because of its availability, low cost, stability, and unusual ligand-binding properties, serum albumin has been one of the most extensively studied and applied proteins in biochemistry. However, as a protein, albumin is far from typical, and the widespread interest in and application of albumin have not been balanced by an understanding of its molecular structure. Indeed, for more than 30 years structural information was surmised based solely on techniques such as hydrodynamics, low-angle X-ray scattering, and predictive methods. 

The introduction of succinyl residues producing short-range repulsive forces in place of possible short-range attractive forces in the native molecule resulted in a change of hydrodynamic properties of bovine serum albumin (BSA), bovine y-globulin, and /3-lactoglobulin [3], The succinylated derivatives showed markedly increased intrinsic viscosity and Stokes radius and a decrease of sedimentation coefficient [36,37], These results are compatible only with a considerable increase in the effective volume occupied by the succinylated protein molecule compared to its unreacted counterpart. 

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