Immobilization of trypsin on carbon
β Scribed by G. E. Stoner; E. Gileadi; J. C. Ludlow; D. J. Kirwan
- Publisher
- John Wiley and Sons
- Year
- 1975
- Tongue
- English
- Weight
- 80 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-3592
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## Abstract Trypsin was coupled on an agarose gel which was modified with a spiropyran compound. The trypsinβspiropyran (agarose) gel showed reverse photochromism. The activity of the trypsinβspiropyran gel in the dark was 12% of that of native trypsin, and it was higher than that under visible lig
## Abstract Trypsin was immobilized in quasiβsoluble polyanionβpolycation complexes with retention of the enzyme activity. The activity of the immobilized enzyme strongly depends on pH of the prepared solution, composition, relative concentrations and molar masses of the polyelectrolytes. The highe