Hydrogen-deuterium exchange mass spectrometry reveals three unique binding responses of mAbs directed to the catalytic domain of hCAIX

Hydrogen-deuterium exchange mass spectrometry reveals three unique binding responses of mAbs directed to the catalytic domain of hCAIX

Human carbonic anhydrase (hCAIX), an extracellular enzyme that catalyzes the reversible hydration of CO2, is often overexpressed in solid tumors. This enzyme is instrumental in maintaining the survival of cancer cells in a hypoxic and acidic tumor microenvironment. Absent in most normal tissues, hCA...

Full description

Bibliographic Details
Main Authors: Joey G. Sheff, John F. Kelly, Anna Robotham, Traian Sulea, Félix Malenfant, Denis L’Abbé, Mélanie Duchesne, Alex Pelletier, Jean Lefebvre, Andrea Acel, Marie Parat, Mylene Gosselin, Cunle Wu, Yves Fortin, Jason Baardsnes, Henk Van Faassen, Shannon Awrey, Shawn C. Chafe, Paul C. McDonald, Shoukat Dedhar, Anne E.G. Lenferink
Format: Article
Language:English
Published: Taylor & Francis Group 2021-01-01
Series:mAbs
Subjects:
Carbonic anhydrase
hydrogen-deuterium exchange
mass spectrometry
epitope mapping
anti-cancer target
antibody-drug conjugate
Online Access:https://www.tandfonline.com/doi/10.1080/19420862.2021.1997072

Internet

https://www.tandfonline.com/doi/10.1080/19420862.2021.1997072

Similar Items