Comparative characteristics of chymotrypsin covalently bound on chemically and enzymatically oxidized agaroses
✍ Scribed by Kamen Voivodov; Nikolina Stambolieva; Jaroslava Turkova
- Publisher
- Springer-Verlag
- Year
- 1991
- Tongue
- English
- Weight
- 191 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0951-208X
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✦ Synopsis
The enzymatically activated agaroses compared with chemically activated show 25 fold lower amount of generated aldehyde groups, 33 fold lower binding capacity for chymotrypsin, 3 fold lower proteolytic as well as amidolytic activity toward AntAlaAlaPheNA of the corresponding fixed enzyme. Tran#-cinnamoylimidazole titration data demonstrate 100% active bound enzyme in the case of enzymatically oxidized agaroses and 57% for chemically oxidized_ The enzymic activation offers a small number of sites for ligand attachment in a unique microenvironment. The chemical activation yields a suitable matrix for effective chymotrypsin immobilization.