Development of a multidimensional online method for the characterization and quantification of monoclonal antibodies using immobilized flow-through enzyme reactors

Author(s):  
Lars M. H. Reinders ◽  
Martin D. Klassen ◽  
Thorsten Teutenberg ◽  
Martin Jaeger ◽  
Torsten C. Schmidt
2001 ◽  
Vol 16 (6) ◽  
pp. 391-397 ◽  
Author(s):  
S. Böhm ◽  
D. Pijanowska ◽  
W. Olthuis ◽  
P. Bergveld

1996 ◽  
Vol 8 (12) ◽  
pp. 1135-1139 ◽  
Author(s):  
Ulrich Rüdel ◽  
Oliver Geschke ◽  
Karl Cammann

2010 ◽  
Vol 85 (1) ◽  
pp. 1-6 ◽  
Author(s):  
S. Janardhan ◽  
P. Pandiaraja ◽  
V. Pandey ◽  
A. Karande ◽  
P. Kaliraj

AbstractThe importance of developing effective assays to diagnose, monitor and evaluate human lymphatic filariasis has been emphasized by the World Health Organization. Presently, few immunodiagnostics are available for filarial monitoring programmes. The Wuchereria bancrofti (Wb) SXP-1 parasite protein, with 84% homology to Brugia malayi (Bm) SXP-1, was found to be highly immunogenic. WbSXP-1 is one among the diagnostic candidate molecules that were used for developing a rapid-antibody-flow-through diagnostic kit for filariasis. Studies were initiated with the aim of developing monoclonal antibodies against recombinant WbSXP-1 and prospective applications for the detection of both circulating Wb and Bm antigens in serum samples from infected individuals. The monoclones 1A6C2 of subclass IgG1k, and 2A12F8 of class IgM, specifically detected Wb and Bm microfilaria isolated from patients and did not show cross-reactivity with other filarial recombinant antigens. We anticipate that this work will address the problems faced in the rapid diagnosis of human lymphatic filariasis in endemic areas in developing countries.


2020 ◽  
Vol 22 (12) ◽  
pp. 3727-3733 ◽  
Author(s):  
Mohamed Baccour ◽  
Alexandra Lamotte ◽  
Kento Sakai ◽  
Eric Dubreucq ◽  
Ahmad Mehdi ◽  
...  

A flow-through bi-enzymatic reactor was developed to produce formate from carbon dioxide gas (CO2).


mAbs ◽  
2018 ◽  
Vol 10 (2) ◽  
pp. 325-334 ◽  
Author(s):  
Takamitsu Ichihara ◽  
Takao ITO ◽  
Yasuhiko Kurisu ◽  
Kevin Galipeau ◽  
Christopher Gillespie

2021 ◽  
Vol 8 ◽  
Author(s):  
Francesca Rinaldi ◽  
Sara Tengattini ◽  
Gloria Brusotti ◽  
Giuseppe Tripodo ◽  
Benjamin Peters ◽  
...  

The characterization of monoclonal antibodies (mAbs) requires laborious and time-consuming sample preparation steps before the liquid chromatography–mass spectrometry (LC-MS) analysis. Middle-up approaches entailing the use of specific proteases (papain, IdeS, etc.) emerged as practical and informative methods for mAb characterization. This work reports the development of immobilized enzyme reactors (IMERs) based on papain able to support mAb analytical characterization. Two monolithic IMERs were prepared by the covalent immobilization of papain on different supports, both functionalized via epoxy groups: a Chromolith® WP 300 Epoxy silica column from Merck KGaA and a polymerized high internal phase emulsion (polyHIPE) material synthesized by our research group. The two bioreactors were included in an in-flow system and characterized in terms of immobilization yield, kinetics, activity, and stability using Nα-benzoyl-L-arginine ethyl ester (BAEE) as a standard substrate. Moreover, the two bioreactors were tested toward a standard mAb, namely, rituximab (RTX). An on-line platform for mAb sample preparation and analysis with minimal operator manipulation was developed with both IMERs, allowing to reduce enzyme consumption and to improve repeatability compared to in-batch reactions. The site-specificity of papain was maintained after its immobilization on silica and polyHIPE monolithic supports, and the two IMERs were successfully applied to RTX digestion for its structural characterization by LC-MS. The main pros and cons of the two supports for the present application were described.


2017 ◽  
Vol 1061-1062 ◽  
pp. 110-116 ◽  
Author(s):  
Tsuyoshi Yamada ◽  
Koichi Yamamoto ◽  
Takashi Ishihara ◽  
Shigeru Ohta

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