Fast analysis of recombinant monoclonal antibodies using IdeS proteolytic digestion and electrospray mass spectrometry

2011 ◽  
Vol 415 (2) ◽  
pp. 212-214 ◽  
Author(s):  
Guillaume Chevreux ◽  
Nolwenn Tilly ◽  
Nicolas Bihoreau
Keyword(s):  
Mass Spectrometry ◽  
Monoclonal Antibodies ◽  
Electrospray Mass Spectrometry ◽  
Proteolytic Digestion ◽  
Fast Analysis

Analysis of Trace Level Perchlorate in Drinking Water and Ground Water by Electrospray Mass Spectrometry

1998 ◽  
Author(s):  
Rebecca A. Clewell ◽  
Wayne T. Brashear ◽  
David T. Tsui ◽  
Sanwat Chaudhuri ◽  
Rachel S. Cassady
Keyword(s):  
Mass Spectrometry ◽  
Drinking Water ◽  
Ground Water ◽  
Electrospray Mass Spectrometry ◽  
Trace Level

scholarly journals Development of a New Highly Selective Monoclonal Antibody against Preferentially Expressed Antigen in Melanoma (PRAME) and Identification of the Target Epitope by Bio-Layer Interferometry

2021 ◽  
Vol 22 (6) ◽  
pp. 3166
Author(s):  
Jwala Priyadarsini Sivaccumar ◽  
Antonio Leonardi ◽  
Emanuela Iaccarino ◽  
Giusy Corvino ◽  
Luca Sanguigno ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Western Blotting ◽  
Cancer Biomarkers ◽  
Trypsin Digestion ◽  
Protein Fragments ◽  
Target Epitope ◽  
Potential Activity ◽  
Antibody Epitopes

Background: Monoclonal antibodies (mAbs) against cancer biomarkers are key reagents in diagnosis and therapy. One such relevant biomarker is a preferentially expressed antigen in melanoma (PRAME) that is selectively expressed in many tumors. Knowing mAb’s epitope is of utmost importance for understanding the potential activity and therapeutic prospective of the reagents. Methods: We generated a mAb against PRAME immunizing mice with PRAME fragment 161–415; the affinity of the antibody for the protein was evaluated by ELISA and SPR, and its ability to detect the protein in cells was probed by cytofluorimetry and Western blotting experiments. The antibody epitope was identified immobilizing the mAb on bio-layer interferometry (BLI) sensor chip, capturing protein fragments obtained following trypsin digestion and performing mass spectrometry analyses. Results: A mAb against PRAME with an affinity of 35 pM was obtained and characterized. Its epitope on PRAME was localized on residues 202–212, taking advantage of the low volumes and lack of fluidics underlying the BLI settings. Conclusions: The new anti-PRAME mAb recognizes the folded protein on the surface of cell membranes suggesting that the antibody’s epitope is well exposed. BLI sensor chips can be used to identify antibody epitopes.

Determination of the endogenous phosphorylation state of B-50/GAP-43 and neurogranin in different brain regions by electrospray mass spectrometry

FEBS Letters ◽  
1996 ◽  
Vol 389 (3) ◽  
pp. 309-313 ◽  
Author(s):  
Monica Di Luca ◽  
Lucia Pastorino ◽  
Vittorio Raverdino ◽  
Pierre N.E. De Graan ◽  
Antonio Caputi ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Mass Spectrometry ◽  
Brain Regions ◽  
Phosphorylation State
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