Journal:

Article Title: Discovery and Characterization of a Peptide Motif That Specifically Recognizes a Non-native Conformation of Human IgG Induced by Acidic pH Conditions * S⃞

doi: 10.1074/jbc.M807618200

Figure Lengend Snippet: The binding properties of the acid conformer to Protein A, antigen and Fcγ receptors. A, inhibition of the binding between the type II peptide and the acid conformer by Protein A. Acid-treated MRA (660 nm) was injected to the type II peptide (IMG4K6R)-immobilized sensor chip in the presence of several concentrations of Protein A (0-24 μm). At the time indicated by the arrow (450 s), the injection phase was stopped and the cells were washed with HBS buffer. B, antigen- and receptor-binding properties of the acid conformer trapped on the type II peptide-immobilized sensor chip. Acid-treated MRA (660 nm) was trapped on the sensor chip at 2200 RU. The antigen (human IL-6R) or FcγR (human FcγRIa, FcγRIIb, or FcγRIIIa) was subsequently injected at each concentration (times indicated by arrows). C, schematic diagram of human IgG. Acid treatment induces conformational changes on the Fc region but not on the Fabs or antigen binding region.

Article Snippet: Recombinant human Fcγ receptor (FcγR) Ia, IIb, and IIIa were purchased from Abnova Corporation, Taipei, Taiwan.

Techniques: Binding Assay, Inhibition, Injection, Concentration Assay