Bio-mass spectrometry

Since 2012 we operate a high-resolution Q-TOF mass spec (Bruker, Maxis G4) (as partner of the EQ-VIBT GmbH) and an ion-trap with CID and ETD capability (Bruker, amaZone Speed ETD) plus the necessary nano- and capillary HPLC systems. The high resolution, mass accuracy and sensitivity allow to answer an infinite variety of analytical problems such as protein identification via peptide mapping, de novo sequencing of peptides, mass determination of intact proteins and last but not least quantitative proteomics.  These capacities are regularily drawn on by other groups from BOKU and elsewhere.

Glycoprotein analysis

Oligosaccharides on secreted proteins are highly complex and diverse structures, which differ by the number and position/linkage of several different sugar residues. We develop methods for a true isomer-sensible glycan analysis using our modern LC-MS equipment to the best. Reference glycans are synthetized using recombinant glycosyltransferases. Our curiosity leads us into the kingdoms of plants, insects, algae and fungi. Most efforts are however dedicated to pharmaceutically relevant glycoproteins.

A particular focus is on the development of appropriate methods for mining the enormous piles of data provided by LC-MS analysis in the field of glycoproteomics and glycomics. The self-developed programs can be found in the "Stadlmann Lab".

Glycan biosynthesis 

Plant O-glycans and their biosynthesis are an as of yet still rather unexplored area. Our research with plant O-glycans arose with the discovery of such structures on weed pollen allergens. Additionally, it is the increasing use of plants as expression systems that demands a better understanding of these post-translational modifications via a combination of analytical, biological and immunogical techniques.


The sugar residues on glycoproteins of different species often exhibit “foreign” structures and are thus immunogenic. On allergens of pollens, insect venoms or vegetable foodstuffs glycans contribute to IgE binding – a phenomen that contributes considerably to apparent cross-reactivity in serum-based allergy diagnosis. We developed a simple, cheap and robust means of eliminating these false positive measurements. This research area has led to the  spin-off proglycan, which strives to implement a simple and cost-effective solution in worldwide diagnostic practice.