𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Improved Pharmacokinetics Properties for Catalase by Site-Specific Glycosidation with Aminated Dextran

✍ Scribed by Yunel Pérez; Aymara Valdivia; Hector L. Ramírez; Reynaldo Villalonga

Publisher
John Wiley and Sons
Year
2005
Tongue
English
Weight
162 KB
Volume
26
Category
Article
ISSN
1022-1336

No coin nor oath required. For personal study only.

✦ Synopsis

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 catalase, increasing by 7.8‐ and 20‐fold the plasma half‐life times for the α and β phases, and reducing by 176‐fold the total clearance after intravenous administration in rats.

Schematic of the catalase dextran conjugate synthesized here.

imageSchematic of the catalase dextran conjugate synthesized here.

📜 SIMILAR VOLUMES

Improved pharmacokinetics and stability
Improved pharmacokinetics and stability properties of catalase by chemical glycosidation with end-group activated dextran
✍ Reynaldo Villalonga; Aymara Valdivia; Yunel Pérez; Bertha Chongo 📂 Article 📅 2006 🏛 John Wiley and Sons 🌐 English ⚖ 70 KB

## 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 increase

Improved Anti-Inflammatory and Pharmacok
Improved Anti-Inflammatory and Pharmacokinetic Properties for Superoxide Dismutase by Chemical Glycosidation with Carboxymethylchitin
✍ Aimara Valdivia; Yunel Perez; Amalia Dominguez; Julio Caballero; Leissy Gomez; E 📂 Article 📅 2005 🏛 John Wiley and Sons 🌐 English ⚖ 114 KB

## Abstract **Summary:** __O__‐Carboxymethylchitin (molecular weight = 1.07 × 10^5^, degree of carboxymethylation = 80%, degree of __N__‐acetylation = 91%) was chemically attached to superoxide dismutase by the formation of amide linkages through a carbodiimide catalyzed reaction. The glycosidated