scholarly journals Characterization of Excipient Effects on Reversible Self-Association, Backbone Flexibility, and Solution Properties of an IgG1 Monoclonal Antibody at High Concentrations: Part 1

2020 ◽  
Vol 109 (1) ◽  
pp. 340-352 ◽  
Author(s):  
Yue Hu ◽  
Jayant Arora ◽  
Sangeeta B. Joshi ◽  
Reza Esfandiary ◽  
C. Russell Middaugh ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Solution Properties ◽  
Backbone Flexibility ◽  
Igg1 Monoclonal Antibody ◽  
Self Association ◽  
High Concentrations

scholarly journals Characterization of Native Reversible Self-Association of a Monoclonal Antibody Mediated by Fab-Fab Interaction

2020 ◽  
Vol 109 (1) ◽  
pp. 443-451 ◽  
Author(s):  
Lorenzo Gentiluomo ◽  
Dierk Roessner ◽  
Werner Streicher ◽  
Sujata Mahapatra ◽  
Pernille Harris ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Self Association

scholarly journals Characterization of the binding epitope of a monoclonal antibody to sulphatide

1988 ◽  
Vol 251 (1) ◽  
pp. 17-22 ◽  
Author(s):  
P Fredman ◽  
L Mattsson ◽  
K Andersson ◽  
P Davidsson ◽  
I Ishizuka ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Thin Layer ◽  
Bacterial Membrane ◽  
Hydrophobic Region ◽  
Terminal Galactose ◽  
Igg1 Monoclonal Antibody ◽  
Binding Epitope ◽  
Maximal Binding ◽  
Binding Avidity

An IgG1 monoclonal antibody, Sulph I, reacting with sulphatide (3′-sulphogalactosylceramide), was produced by immunizing Balb/c mice with that glycolipid coated on Salmonella minnesota bacterial membrane. Radioimmunodetection of the binding of the monoclonal antibody to structurally related glycolipids adsorbed to microtitre plates or chromatographed on thin-layer plates was used to determine its binding epitope. The antibody showed similar binding avidity to three sulphated glycolipids: sulphatide, sulpholactosylceramide and seminolipid. Lysosulphatide did bind the antibody, but, compared with sulphatide, 30 times more antigen was needed for half-maximal binding. Bis(sulphogangliotriosyl)ceramide and bis-sulphogangliotetraosylceramide did not bind the antibody. These results suggest that terminal galactose-3-O-sulphate and part of the hydrophobic region of the glycolipid are recognized by the Sulph I antibody.

scholarly journals Mitigation of reversible self-association and viscosity in a human IgG1 monoclonal antibody by rational, structure-guided Fv engineering

mAbs ◽  
2016 ◽  
Vol 8 (5) ◽  
pp. 941-950 ◽  
Author(s):  
James C. Geoghegan ◽  
Ryan Fleming ◽  
Melissa Damschroder ◽  
Steven M. Bishop ◽  
Hasige A. Sathish ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Rational Structure ◽  
Igg1 Monoclonal Antibody ◽  
Human Igg1 ◽  
Self Association ◽  
Human Igg1 Monoclonal Antibody

scholarly journals Small-Angle Neutron Scattering Characterization of Monoclonal Antibody Conformations and Interactions at High Concentrations

2013 ◽  
Vol 105 (3) ◽  
pp. 720-731 ◽  
Author(s):  
Eric J. Yearley ◽  
Isidro E. Zarraga ◽  
Steven J. Shire ◽  
Thomas M. Scherer ◽  
Yatin Gokarn ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
High Concentrations

Monoclonal Antibody Self-Association, Cluster Formation, and Rheology at High Concentrations

2013 ◽  
Vol 117 (21) ◽  
pp. 6373-6384 ◽  
Author(s):  
Wayne G. Lilyestrom ◽  
Sandeep Yadav ◽  
Steven J. Shire ◽  
Thomas M. Scherer
Keyword(s):  
Monoclonal Antibody ◽  
Cluster Formation ◽  
Self Association ◽  
High Concentrations
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