Thermal inactivation of enzymes and pathogens in biosamples for MS analysis
2015 (English)In: Bioanalysis, ISSN 1757-6180, E-ISSN 1757-6199, Vol. 7, no 15, 1885-1899 p.Article, review/survey (Refereed) Published
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 (approximate to 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.
Place, publisher, year, edition, pages
2015. Vol. 7, no 15, 1885-1899 p.
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:uu:diva-264492DOI: 10.4155/bio.15.122ISI: 000360296400007PubMedID: 26295989OAI: oai:DiVA.org:uu-264492DiVA: diva2:860738