Bovine serum albumin probe diffusion

The urease is incorporated into a polyacrylamide gel which is allowed to set on the bulb of the glass electrode and may be held in position by nylon gauze. Preferably, the urease can be chemically immobilised on to bovine serum albumin or even on to nylon. When the electrode is inserted into a solution containing urea, ammonium ions are produced, diffuse through the gel and cause a response by the ammonium ion probe ... 

Park, et al. [158], observing a benzospiran dye and optically labelled bovine serum albumin via holographic relaxation, found D of the probes depends on matrix concentration and probe size as exp(—3i2 c ). Park, et al., were also able to measure directly the matrix mesh size inferred from the matrix diffusion coeflScient Dc via Dc = kBT/ 6nrj ), T] here being the solvent viscosity they report that Dp is not a universal function of R/ because has the wrong dependence on concentration. 

Phillies reports on the diffusion of bovine serum albumin through solutions of 100 kDa and 300 kDa polyethylene oxides(27). The Dp value depended measurably on the probe concentration. At elevated polymer c and low protein concentration. Dp was as much as a third faster than expected from the c-dependent solution fluidity. With increasing protein concentration. Dp fell toward values expected from the macroscopic r. This study pushed the technical limits of then-current light-scattering instrumentation. 

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