A specific colorimetric assay for measuring transglutaminase 1 and factor XIII activities |
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Authors: | Kiyotaka Hitomi Miyako Kitamura Mileidys Perez Alea Ismail Ceylan Vincent Thomas Saïd El Alaoui |
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Institution: | 1. Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nayoya 464-8601, Japan;2. CovalAb S.A.R.L., 11 Avenue Albert Einstein, 69100 Villeurbanne, France |
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Abstract: | Transglutaminase (TGase) is an enzyme that catalyzes both isopeptide cross-linking and incorporation of primary amines into proteins. Eight TGases have been identified in humans, and each of these TGases has a unique tissue distribution and physiological significance. Although several assays for TGase enzymatic activity have been reported, it has been difficult to establish an assay for discriminating each of these different TGase activities. Using a random peptide library, we recently identified the preferred substrate sequences for three major TGases: TGase 1, TGase 2, and factor XIII. In this study, we use these substrates in specific tests for measuring the activities of TGase 1 and factor XIII. |
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