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Identification of human salivary transglutaminases
Transglutaminases (TGs) expression and enzymatic activities in human saliva were investigated. Specific antibodies showed the co-existence of TG1, TG2, TG3 and TG4. TG2 and TG3 were found in native and multiple proteolytic forms. Our data indicate that TG1 and TG2 isoenzymes are highly active with t...
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Published in: | Amino acids 2013, Vol.44 (1), p.245-250 |
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creator | Perez Alea, Mileidys Thomas, Vincent Martin, Guillaume El Alaoui, Saïd |
description | Transglutaminases (TGs) expression and enzymatic activities in human saliva were investigated. Specific antibodies showed the co-existence of TG1, TG2, TG3 and TG4. TG2 and TG3 were found in native and multiple proteolytic forms. Our data indicate that TG1 and TG2 isoenzymes are highly active with the major activity attributed to TG1. These findings pave the way for future studies on the physiological role of TG in the oral cavity and the potential impact of their deregulation in TG-associated oral diseases. |
doi_str_mv | 10.1007/s00726-011-1142-5 |
format | article |
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Specific antibodies showed the co-existence of TG1, TG2, TG3 and TG4. TG2 and TG3 were found in native and multiple proteolytic forms. Our data indicate that TG1 and TG2 isoenzymes are highly active with the major activity attributed to TG1. 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subjects | Amino acids Analytical Chemistry Antibodies Biochemical Engineering Biochemistry Biomedical and Life Sciences Deregulation Diseases Enzyme Inhibitors - chemistry Female GTP-Binding Proteins Holes Human Humans Isoenzymes - antagonists & inhibitors Isoenzymes - chemistry Isoenzymes - metabolism Life Sciences Male Neurobiology Original Article Peptide Fragments - chemistry Proteomics Saliva Saliva - enzymology Transglutaminases - antagonists & inhibitors Transglutaminases - chemistry Transglutaminases - metabolism |
title | Identification of human salivary transglutaminases |
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