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Fluorescence assessment of antibody binding and molecular interactions

Paper ID Volume ID Publish Year Pages File Format Full-Text
29267 44143 2007 6 PDF Available
Title
Fluorescence assessment of antibody binding and molecular interactions
Abstract

We observed a pronounced decrease in the binding affinity of TMR to the immunoglobulin specific for this dye upon adding β-cyclodextrin. Experimental evidence suggests that TMR interacts simultaneously with the IgG antigen binding site and with the CD cavity. Fluorescence anisotropy was employed to further characterize the nature of the interactions between TMR and IgG. It is found that TMR binds with high affinity to IgG, but retains its ability to rotate within the antigen binding site.

Keywords
TMR, tetramethylrodamine; CD, β-cyclodextrin; IgG, immunoglobulin; CCVJ, 9-(2-carboxy 2-cyanovinyl)julolidine; Fab, fragment binding antigen; Fc, fragment crystallizableImmunoglobuling affinity; Cyclodextrins
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Fluorescence assessment of antibody binding and molecular interactions
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 189, Issues 2–3, 25 June 2007, Pages 218–223
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
You save - $31
Price after discount Only $4.95
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