| Title | A Specific Colorimetric Assay for Measuring of Transglutaminase 1 and Factor XIII Activities. | | Author(s) | Hitomi K, Kitamura M, Alea MP, Ceylan I, Thomas V, Alaoui SD | | Institution | Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, 464-8601, Japan. | | Source | Anal Biochem 2009 Jul 29. | | Abstract | Transglutaminase (TGase) is an enzyme that catalyses both isopeptide cross-linking and incorporation of primary amines into proteins. Eight TGases have been identified in human, each of which 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. | | Language | ENG | | Pub Type(s) | JOURNAL ARTICLE
| | PubMed ID | 19646949 |
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