Immunological detection of proteolytically activated epidermal-type transglutaminase (TGase 3) using cleavage-site-specific antibody.
Transglutaminase 3 (TGase 3), involved in the cross-linking of structural proteins in the epidermis, is activated by limited proteolysis of zymogen into two fragments during keratinocyte differentiation. Using recombinant TGase 3, the N-terminus sequence of the proteolyzed fragment was analyzed. Antibody against the synthetic peptide corresponding to the cleavage site specifically detected the fragment in the mouse forestomach extract.
Hitomi
Kiyotaka
K
Department of Applied Molecular Biological Sciences, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Japan. hitomi@agr.nagoya-u.ac.jp
Ikeda
Naoki
N
Maki
Masatoshi
M
D000818:Animals; D015153:Blotting, Western; D002135:Calcium-Binding Proteins / Q000032:analysis*; D005753:Gastric Mucosa / Q000201:enzymology; D007118:Immunoassay; D015603:Keratinocytes / Q000201:enzymology; D051379:Mice; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry; D011503:Transglutaminases / Q000032:analysis*
D002135:Calcium-Binding Proteins; D010446:Peptide Fragments; C498713:Tgm3 protein, mouse; D011503:Transglutaminases