Foam fractionation of proteins: Concentration of aqueous solutions of bovine serum albumin
โ Scribed by Schnepf, Robert W. ;Gaden, Elmer L.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1959
- Weight
- 470 KB
- Volume
- 1
- Category
- Article
- ISSN
- 0368-1467
No coin nor oath required. For personal study only.
โฆ Synopsis
Abstract
The effects of pH and concentration on foam separation of the protein bovine serum albumin (BSA) from solution has been studied. All results agree, at least qualitatively, with theory. BSA maximum enrichments were observed at the isoelectric pH and enrichment ratio was found to increase with decreasing protein concentrations.
๐ SIMILAR VOLUMES
Previously Vilker et al. (J. Colloid Interface Sci. 79(2), (1981)) reported the osmotic pressure of concentrated bovine serum albumin (BSA) up to 475 g/L in 0.15 M sodium chloride at pH 4.5, 5.4, and 7.4. The authors used a semiempirical model based on Donnan theory to predict the osmotic pressure w
## Abstract Nonionic and ionic surfactants diminish the initial rate of proteolysis of aqueous bovine serum albumin (BSA) by subtilisin Carlsberg. Surfactants studied include: nonionic tetraethylene glycol monododecyl ether (C~12~E~4~); anionic sodium dodecyl sulfate (SDS), anionic sodium dodecylbe
We report static and dynamic light scattering measurements on bovine serum albumin (BSA) solutions at high ionic strength (I) where potential and hydrodynamic interactions between BSA molecules are of comparable strengths. Measurements of the concentration dependence of the osmotic compressibility,
The purpose of the study was to characterize mucosal attachment of a cationized model protein, bovine serum albumin (BSA), onto the various fractions of colonic crypts epithelium in the rat. BSA was labeled with ยฏuorescein isothiocyanate (FITC) and its surface net electric charge was modiยฎed from ne