title: Thermal inactivation of enzymes and pathogens in biosamples for MS analysis.
abstract: Protein denaturation is the common basis for enzyme inactivation and inactivation of pathogens, necessary for preservation and safe handling of biosamples for downstream analysis. While heat-stabilization technology has been used in proteomic and peptidomic research since its introduction in 2009, the advantages of using the technique for simultaneous pathogen inactivation have only recently been addressed. The time required for enzyme inactivation by heat (≈1 min) is short compared with chemical treatments, and inactivation is irreversible in contrast to freezing. Heat stabilization thus facilitates mass spectrometric studies of biomolecules with a fast conversion rate, and expands the chemical space of potential biomarkers to include more short-lived entities, such as phosphorylated proteins, in tissue samples as well as whole-blood (dried blood sample) samples.
authors: Department of Chemistry & Molecular Biology, University of Gothenburg, SE-412 96 Gothenburg, Sweden.|Denator AB, Göteborg, Sweden.
authors: Martin
authors: M
authors: Ahnoff
authors: Molecular & Translational Sciences, United States Army Medical Research Institute of Infectious Disease, 1425 Porter St. Frederick, MD 21702, USA.|DoD Biotechnology High Performance Computing Software Applications Institute, Telemedicine & Advanced Technology Research Center, US Army Medical Research and Materiel Command, Fort Detrick, MD 21702, USA.
authors: Lisa H
authors: LH
authors: Cazares
authors: Denator AB, Göteborg, Sweden.|Department of Medical Sciences, Cancer Pharmacology & Computational Medicine, University of Uppsala, Uppsala, Sweden.
authors: Karl
authors: K
authors: Sköld
mesh_terms: D013058:Mass Spectrometry / Q000379:methods*; D011489:Protein Denaturation; D040901:Proteomics / Q000379:methods*; D016707:Tissue Fixation