caa a22 4500 397558074 CHVBK 20180308164808.0 cr unu---uuuuu 161202e199610 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021491 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021491 Purification and Characterization of a Novel Isoform of Mast Cell Tryptase from Rat Tongue [Elektronische Daten] [Yuushi Okumura, Asako Kudoh, Miwa Takashima, Masahiro Inoue, Kentaro Sakai, Hiroshi Kido] Rat mast cell tryptase was purified to homogeneity from rat tongue by a series of standard chromatographic procedures. Since the enzyme gave band corresponding to molecular mass of 32-35 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis and exhibited a molecular mass of 135 kDa on gel filtration, it was presumed to be a noncovalently associated tetramer. The N-terminal amino acid sequence of 50 residues of the enzyme showed the highest degree of homology with the same region in mouse mast cell protease 7 (92%), and less homology to those of tryptases from man and dog, and peritoneal cells of rats and Mongolian gerbils. The inhibitor specificity of rat tongue tryptase was similar to that of rat peritoneal mast cell tryptase free from trypstatin: it was inhibited by α1-antitrypsin, Kunitz-type soybean trypsin inhibitor and Bowman-Birk soybean trypsin inhibitor, but these inhibitors do not inhibit the tryptases from rat skin, human lung, and dog mast cells. Judging from these results, together with other enzymatic properties, the enzyme may be a novel isoform of tryptase in rat tongue. Analysis by differential staining with peroxidaselabeled lectins of the enzyme suggested that it has tri- and/or tetraantennary complex-type oligosaccharides containing a relatively high amount of sialic acid. The immunohistochemical distribution of this enzyme indicated that the reactive antigen was specific in connective tissue but not in mucosal mast cells. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence glycosylation nationallicence mast cell nationallicence N-terminal amino acid sequence nationallicence rat tongue nationallicence tryptase nationallicence Okumura Yuushi Division of Enzyme Chemistry, Institute for Enzyme Research Kuramoto-cho 18-15, Tokushima, Tokushima 770 aut Kudoh Asako Division of Enzyme Chemistry, Institute for Enzyme Research Kuramoto-cho 18-15, Tokushima, Tokushima 770 aut Takashima Miwa Division of Enzyme Chemistry, Institute for Enzyme Research Kuramoto-cho 18-15, Tokushima, Tokushima 770 aut Inoue Masahiro Division of Enzyme Chemistry, Institute for Enzyme Research Kuramoto-cho 18-15, Tokushima, Tokushima 770 aut Sakai Kentaro Department of Nutrition, School of Medicine, The University of Tokushima Kuramoto-cho 18-15, Tokushima, Tokushima 770 aut Kido Hiroshi Division of Enzyme Chemistry, Institute for Enzyme Research Kuramoto-cho 18-15, Tokushima, Tokushima 770 aut The Journal of Biochemistry Oxford University Press 120/4(1996-10), 856-864 0021-924X 120:4<856 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021491 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021491 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Okumura Yuushi Division of Enzyme Chemistry, Institute for Enzyme Research Kuramoto-cho 18-15, Tokushima, Tokushima 770 aut NATIONALLICENCE 700 1- Kudoh Asako Division of Enzyme Chemistry, Institute for Enzyme Research Kuramoto-cho 18-15, Tokushima, Tokushima 770 aut NATIONALLICENCE 700 1- Takashima Miwa Division of Enzyme Chemistry, Institute for Enzyme Research Kuramoto-cho 18-15, Tokushima, Tokushima 770 aut NATIONALLICENCE 700 1- Inoue Masahiro Division of Enzyme Chemistry, Institute for Enzyme Research Kuramoto-cho 18-15, Tokushima, Tokushima 770 aut NATIONALLICENCE 700 1- Sakai Kentaro Department of Nutrition, School of Medicine, The University of Tokushima Kuramoto-cho 18-15, Tokushima, Tokushima 770 aut NATIONALLICENCE 700 1- Kido Hiroshi Division of Enzyme Chemistry, Institute for Enzyme Research Kuramoto-cho 18-15, Tokushima, Tokushima 770 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/4(1996-10), 856-864 0021-924X 120:4<856 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford