## Abstract **Summary:** Catalase was chemically modified with an end‐group aminated dextran derivative via a carbodiimide catalyzed reaction. The enzymatic activity of catalase was increased after glycosidation with 4 mol of polymer. This modification improved the pharmacokinetic behavior of catal
Improved pharmacokinetics and stability properties of catalase by chemical glycosidation with end-group activated dextran
✍ Scribed by Reynaldo Villalonga; Aymara Valdivia; Yunel Pérez; Bertha Chongo
- Publisher
- John Wiley and Sons
- Year
- 2006
- Tongue
- English
- Weight
- 70 KB
- Volume
- 102
- Category
- Article
- ISSN
- 0021-8995
No coin nor oath required. For personal study only.
✦ Synopsis
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 3‐fold more resistant to tryptic degradation. The plasma half‐life time was increased to 7.3‐fold after glycosidation. © 2006 Wiley Periodicals, Inc. J Appl Polym Sci 102: 4573–4576, 2006
📜 SIMILAR VOLUMES
## Abstract **Summary:** Bovine Cu,Zn‐SOD was chemically modified with an end‐group aminated dextran derivative using a water‐soluble carbodiimide as coupling agent. The enzyme retained 81% of the initial catalytic activity after the attachment of about 4.4 mol of polymer per protein subunit. The a