Stabilization of catalase by covalent attachment to dextran
β Scribed by J. John Marshall; Mark L. Rabinowitz
- Publisher
- John Wiley and Sons
- Year
- 1976
- Tongue
- English
- Weight
- 261 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0006-3592
No coin nor oath required. For personal study only.
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## Abstract Catalase was chemically modified with a monoactivated dextran derivative having a carboxylate group at its reducing end residue. The modified enzyme retained 77% of its initial specific activity and was 3βfold more resistant to tryptic degradation. The plasma halfβlife time was increase
## Abstract Several covalent attachment chemistries were tested for the immobilization of DNA onto glass beads. The comparison was based on the ability of these chemistries to produce derivatized beads that give good hybridization signals. Cyanuric chloride, isothiocyanate, nitrophenyl chloroformat