Microcalorimetric Study on the Oscillating System of Two-phase Reaction of Aqueous Acid with Primary Amine in Chloroform
β Scribed by Zhang Hong-Lin; Yu Xiu-Fang; Lu Cheng-Xue; Sun Si-Xiu; Gu Guo-Hna; Fu Xim
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 236 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0256-7660
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π SIMILAR VOLUMES
Relatively conservative modifications of three proteins were carried out to alter their surface properties. The protein properties modified were hydrophobicity and charge. This was done by acylation of amino groups with anhydrides. For the hydrophobic modification experiments, two proteins (p-lactog
Two different series of hydrophobically modified proteins were partitioned in a number of aqueous two-phase systems (ATPS) to investigate the effect of hydrophobicity as a single property on partitioning. The modified proteins were derived from P-lactoglobulin and bovine serum albumin (BSA). Measure
A series of charge-modified thaumatins with different values of surface charge were partitioned in aqueous twophase systems (ATPS) to study the effect of surface charge as a single property on partitioning. Electrophoretic mobility of the proteins in titration curves was used as a measure of surface
## Abstract The behavior of a series of pure proteins partitioned in aqueous twoβphase systems is compared with their behavior during mild hydrophobic interaction chromatography (HIC). A simple theoretical rationale for this comparison is presented based upon solvophobic theory. Similarities were f