Selective separation of trypsin from a mixture involving many kinds of contaminating proteins, i.e., pancreatin, was achieved using trypsin inhibitor immobilized in the reverse micelles, which were composed of a nonionic surfactant, tetra-oxyethylene monodecylether. To determine the efficient operat
โฆ LIBER โฆ
Bioaffinity separation of chymotrypsinogen using antigen-antibody reaction in reverse micellar system composed of a nonionic surfactant
โ Scribed by Motonari Adachi; Makoto Harada; Shigeo Katoh
- Book ID
- 104420334
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- English
- Weight
- 61 KB
- Volume
- 4
- Category
- Article
- ISSN
- 1369-703X
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Trypsin inhibitor was converted to hydrophobic states by covalently combining cholesteryl groups using an acylation reaction, and was immobilized in reverse micelles composed of a nonionic surfactant. Using this reverse micellar phase containing trypsin inhibitor as an affinity ligand, trypsin was s