Influence of surface structure on the ion exchange of proteins—The effect of protein charge on uptake of acid proteases
✍ Scribed by Alfred Carlson
- Publisher
- Elsevier Science
- Year
- 1987
- Weight
- 739 KB
- Volume
- 6
- Category
- Article
- ISSN
- 0167-6989
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📜 SIMILAR VOLUMES
A survey of hydrophobic patches on the surface of 112 soluble, monomeric proteins is presented. The largest patch on each individual protein averages around 400 A2 but can range from 200 to 1,200 A2. These areas are not correlated to the sizes of the proteins and only weakly to their apolar surface
## Abstract Dynamic binding capacity (DBC) decreases with increasing conductivity in the equilibrium regime for ion exchange chromatography. An exclusion regime has been demonstrated in ion exchange resins where DBC increases with increasing conductivity and decreasing protein charge. The purpose o
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