A specific colorimetric assay for measuring transglutaminase 1 and factor XIII activities.
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.
Hitomi
Kiyotaka
K
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nayoya 464-8601, Japan. hitomi@agr.nagoya-u.ac.jp
Kitamura
Miyako
M
Alea
Mileidys Perez
MP
Ceylan
Ismail
I
Thomas
Vincent
V
El Alaoui
Saïd
S
D000595:Amino Acid Sequence; D001681:Biological Assay; D019921:Biotinylation; D003124:Colorimetry; D005176:Factor XIII / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D019151:Peptide Library; D011485:Protein Binding / Q000235:genetics; D012680:Sensitivity and Specificity; D013379:Substrate Specificity / Q000235:genetics; D013997:Time Factors; D011503:Transglutaminases / Q000032:analysis* / Q000235:genetics / Q000378:metabolism
D019151:Peptide Library; D005176:Factor XIII; D011503:Transglutaminases; C105804:transglutaminase 1