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Real-time fluorescence assay for monitoring transglutaminase activity

Adamczyk, Magdalena, Heil, Andreas and Aeschlimann, Daniel 2013. Real-time fluorescence assay for monitoring transglutaminase activity. Application Notes from BMG Labtech , 234.

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Abstract

Transglutaminases (TGs) form a family of enzymes that catalyze various posttranslational protein modifications such as crosslinking, esterification and deamidation in a Ca2+-dependent manner.(1) Their main function is the formation of covalent Nε-(γ-glutamyl)lysine bonds within or between polypeptides to stabilize protein assemblies. The activity of these enzymes is crucial for tissue homeostasis and function in a number of organ systems, and the lack of or the excessive crosslinking activity have been linked to human disease processes(1,2). Here we perform kinetic measurements using recombinant TG2 and a fluorescent peptide model substrate on a FLUOstar OPTIMA and FLUOstar Omega in a format suitable for high-throughput analysis. This assay principle can be applied to kinetic studies on closely related enzymes including TG6(3) and can be optimised by modification of the backbone peptide sequence.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Dentistry
Subjects: Q Science > Q Science (General)
Q Science > QH Natural history > QH301 Biology
Publisher: BMG Labtech
Funders: Arthritis Research UK, Coeliac UK, EPSRC
Related URLs:
Last Modified: 13 May 2019 19:57
URI: http://orca.cf.ac.uk/id/eprint/47001

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