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

• Main Authors: Joey G. Sheff (Author), John F. Kelly (Author), Anna Robotham (Author), Traian Sulea (Author), Félix Malenfant (Author), Denis L'Abbé (Author), Mélanie Duchesne (Author), Alex Pelletier (Author), Jean Lefebvre (Author), Andrea Acel (Author), Marie Parat (Author), Mylene Gosselin (Author), Cunle Wu (Author), Yves Fortin (Author), Jason Baardsnes (Author), Henk Van Faassen (Author), Shannon Awrey (Author), Shawn C. Chafe (Author), Paul C. McDonald (Author), Shoukat Dedhar (Author), Anne E.G. Lenferink (Author)
• Format: Book
• Published: Taylor & Francis Group, 2021-01-01T00:00:00Z.
• Subjects: article
• Online Access: Connect to this object online.

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...