𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Analysis of glycoforms on the glycosylation site and the glycans in monoclonal antibody biopharmaceuticals

✍ Scribed by Ebru Uçaktürk

Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
186 KB
Volume
35
Category
Article
ISSN
1615-9306

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

Therapeutic monoclonal antibodies (mAbs), immunoglobulins, have been efficiently used in the treatment of many diseases, such as cancer, inflammatory and cardiovascular diseases, and organ transplantation. mAbs are glycoprotein molecules undergoing posttranslational modifications. Glycosylation is one of the posttranslational modifications. Different glycoforms that are important for maintaining the potency of mAb drugs show various biological activities. Therefore, the profile of the glycans and glycosylation sites should be determined to produce safe, good quality, consistent mAb drugs for human use. For this reason, simple, robust, accurate, and reproducible analytical methods need to be developed. In this article, chromatographic methods for the analysis of the glycoforms on the glycosylation site and the glycans in mAb biopharmaceuticals have been evaluated.

📜 SIMILAR VOLUMES

The effect of cosolutes on the isomeriza
The effect of cosolutes on the isomerization of aspartic acid residues and conformational stability in a monoclonal antibody
✍ Aditya A. Wakankar; Jun Liu; David VanderVelde; Y. John Wang; Steven J. Shire; R 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 187 KB 👁 1 views

The aspartate residue (Asp 32) located in the complementarity-determining region (CDR) of a recombinant humanized monoclonal antibody (MAb I) is highly susceptible to the isomerization reaction. The modification of Asp 32 residue due to the isomerization reaction results in a significant reduction i

Near real-time, on-site, quantitative an
Near real-time, on-site, quantitative analysis of PAHs in the aqueous environment using an antibody-based biosensor
✍ Candace R. Spier; George G. Vadas; Stephen L. Kaattari; Michael A. Unger 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 349 KB

## Abstract Rapid, on‐site, quantitative assessments of dissolved polycyclic aromatic hydrocarbons (PAHs) were demonstrated for two field applications. The platform, a KinExA Inline Sensor (Sapidyne Instruments), employed the monoclonal anti‐PAH antibody, 7B2.3, which has specificity for 3‐ to 5‐ri

Epitope mapping of function-blocking mon
Epitope mapping of function-blocking monoclonal antibody CM6 suggests a “weak” integrin binding site on the laminin-332 LG2 domain
✍ Hironobu Yamashita; Meiling Shang; Manisha Tripathi; Jerome Jourquin; Walter Geo 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 406 KB

## Abstract Laminin‐332 (Ln‐332) is an extracellular matrix molecule that regulates cell adhesion, spreading, and migration by interaction with cell surface receptors such as α3β1 and α6β4. Previously, we developed a function‐blocking monoclonal antibody against rat Ln‐332, CM6, which blocks hemide