Hitomi Kiyotaka, Kitamura Miyako, Alea Mileidys Perez, Ceylan Ismail, Thomas Vincent, El Alaoui Saïd
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nayoya 464-8601, Japan.
Anal Biochem. 2009 Nov 15;394(2):281-3. doi: 10.1016/j.ab.2009.07.039. Epub 2009 Jul 30.
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.
转谷氨酰胺酶（TGase）是一种催化异肽交联以及将伯胺掺入蛋白质的酶。在人类中已鉴定出8种转谷氨酰胺酶，并且这些转谷氨酰胺酶中的每一种都具有独特的组织分布和生理意义。尽管已经报道了几种检测转谷氨酰胺酶活性的方法，但很难建立一种区分这些不同转谷氨酰胺酶活性的检测方法。我们最近使用随机肽库确定了三种主要转谷氨酰胺酶（转谷氨酰胺酶1、转谷氨酰胺酶2和因子XIII）的优选底物序列。在本研究中，我们在特定测试中使用这些底物来测量转谷氨酰胺酶1和因子XIII的活性。
