Chemical & Pharmaceutical Structure Analysis
Where Technology and Solutions Meet

CPSA 2011

Science and Technology Coming Together to Make a Difference

October 3 - 6, 2011
Bucks County Sheraton Hotel
Langhorne, PA


Poster Abstract #26

By-products in recombinant TAU protein production characterized by LC-MALDI Top-Down Sequencing (LC-MALDI-TDS)

Arndt Asperger1, Marcus Macht1, Branislav Kovacech2, Andrej Kovac2

1) Bruker Daltonik, Bremen, Germany; 2) Institute of Neuroimmunology of SlovakAcademy of Sciences, Bratislava, Slovakia

Compared to Edman sequencing, MALDI-TOF-MS based top-down sequencing of proteins (MALDI-TDS) is much faster, can deliver significantly longer sequence readouts from both protein N- and C-terminus and has no limitations in case of terminally modified proteins. These features make MALDI-TDS an extremely appealing method for the QC analysis of recombinant protein products, for instance biopharmaceuticals.

Analysis by MALDI-TDS, which uses the in-source decomposition (ISD) of proteins in the MALDI plume, requires purified, homogeneous protein samples as it does not provide for precursor selection. However, coupling MALDI-TDS to upfront LC separation allows to analyze mixtures of proteins.

Recombinant proteins often contain unexpected by-products. As an example, we describe here the characterization of two by-products by LC-MALDI-TDS that occurred in a recombinant TAU protein expression product.

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