## Abstract The adsorption equilibria and kinetics of bovine serum albumin (BSA) and lysozyme to two Cibacron Blue 3GA (CB) modified agarose gels, that is, 6% agaroseโcoated steel (6AS) and Sepharose CLโ6B, in 0.01 kmolยทm^โ3^ trisโHCl buffer (pH 7.5) were studied. Effects of aqueousโphase ionic str
Adsorption equilibrium of proteins on a dye-ligand adsorbent
โ Scribed by Philip M. Boyer; James T. Hsu
- Publisher
- Springer-Verlag
- Year
- 1990
- Tongue
- English
- Weight
- 385 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0951-208X
No coin nor oath required. For personal study only.
โฆ Synopsis
The effect,s of pH and ionic strength on adsorption of lysozyme and bovine serum albumin to Blue Sepharose have been studied. Isotherms for both proteins obey the Freundlich model. Lysozyme binding involves both hydrophobic and cation exchange interactions with the adsorbent, while binding of albumin is due primarily to cation exchange. Protein properties will be discussed in relat,ion to the binding patterns.
๐ SIMILAR VOLUMES
## Abstract The adsorption equilibria of bovine serum albumin (BSA), ฮณโglobulin, and lysozyme to three kinds of Cibacron blue 3GA (CB)โmodified agarose gels, 6% agarose gelโcoated steel heads (6AS), Sepharose CLโ6B, and a homeโmade 4% agarose gel (4AB), were studied. We show that ionic strength has
## Abstract Equilibrium isotherms have been studied for the adsorption of four dyestuffs, namely, Acid Blue 25, Acid Blue 158, Mordant Yellow 5, and Direct Red 84, onto chitin. Langmuir and Freundlich constants have been determined and the effects of chitin particle size and solution temperature ha