The determination of high-affinity protein/inhibitor binding constants by electrospray ionization hydrogen/deuterium exchange mass spectrometry

2006 ◽  
Vol 20 (16) ◽  
pp. 2478-2482 ◽  
Author(s):  
Lee Frego ◽  
Elda Gautschi ◽  
Leslie Martin ◽  
Walter Davidson
Keyword(s):  
Mass Spectrometry ◽  
Binding Constants ◽  
Hydrogen Deuterium Exchange ◽  
Protein Inhibitor ◽  
Inhibitor Binding ◽  
Exchange Mass Spectrometry ◽  
High Affinity ◽  
Hydrogen Deuterium ◽  
Deuterium Exchange Mass Spectrometry

scholarly journals Dataset from HDX-MS Studies of IgG1 Glycoforms and Their Interactions with the FcγRIa (CD64) Receptor

2021 ◽  
Vol 126 ◽  
Author(s):  
Kyle W. Anderson ◽  
Kerry Scott ◽  
Ioannis L. Karageorgos ◽  
Elyssia S. Gallagher ◽  
Tayi Venkata S. ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Human Neutrophils ◽  
Hydrogen Deuterium Exchange ◽  
Exchange Mass Spectrometry ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Hydrogen Deuterium ◽  
Deuterium Exchange Mass Spectrometry ◽  
Affinity Receptor ◽  
Hdx Ms

This document presents hydrogen-deuterium exchange mass spectrometry (HDX-MS) data from measurements of three purified IgG1 glycoform samples, predominantly G0F, G2F, and SAF, in isolation and in complexation with the high-affinity receptor, FcγRIa (CD64). The IgG1 antibody used in this study, aIL8hFc, is a murine-human chimeric IgG1, which inhibits IL-8 binding to human neutrophils.

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