Modeling of protein monomer/aggregate purification and separation using hydrophobic interaction chromatography
✍ Scribed by Justin T. McCue; Philip Engel; Austen Ng; Rich Macniven; Jörg Thömmes
- Book ID
- 106146801
- Publisher
- Springer
- Year
- 2008
- Tongue
- English
- Weight
- 590 KB
- Volume
- 31
- Category
- Article
- ISSN
- 1615-7605
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📜 SIMILAR VOLUMES
To determine whether a Ca2+-activated protein kinase is regulated by calmodulin, it is necessary to separate it from endogenous calmodulin and from protein kinase activity that is not calcium dependent. We describe here a procedure for achieving these goals using Ca2+-dependent hydrophobic interacti
## Abstract The behavior of a series of pure proteins partitioned in aqueous two‐phase 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