메뉴 건너뛰기




Volumn 120, Issue 4, 1996, Pages 856-864

Purification and characterization of a novel isoform of mast cell tryptase from rat tongue

Author keywords

Glycosylation; Mast cell; N terminal amino acid sequence; Rat tongue; Tryptase

Indexed keywords

ALPHA 1 ANTITRYPSIN; ENZYME INHIBITOR; LECTIN; OLIGOSACCHARIDE; PROTEINASE; SIALIC ACID; SOYBEAN TRYPSIN INHIBITOR; TRYPTASE;

EID: 0029811034     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021491     Document Type: Article
Times cited : (7)

References (41)
  • 1
    • 0025141544 scopus 로고
    • New insights into "the riddle of mast cells": Microenvironmental regulation of mast cell development and phenotypic heterogeneity
    • Galli, S.J. (1990) New insights into "the riddle of mast cells": Microenvironmental regulation of mast cell development and phenotypic heterogeneity. Lab. Invest. 82, 5-33
    • (1990) Lab. Invest. , vol.82 , pp. 5-33
    • Galli, S.J.1
  • 2
    • 0019888627 scopus 로고
    • Tryptase from human pulmonary mast cells: Purification and characterization
    • Schwartz, L.B., Lewis, R.A., and Austen, K.F. (1981) Tryptase from human pulmonary mast cells: Purification and characterization. J. Biol. Chem. 266, 11939-11943
    • (1981) J. Biol. Chem. , vol.266 , pp. 11939-11943
    • Schwartz, L.B.1    Lewis, R.A.2    Austen, K.F.3
  • 3
    • 0001409975 scopus 로고
    • A histochemical enzyme kinetic system applied to the trypsin-like amidase and esterase activity in human mast cells
    • Hopsu, V.K. and Glenner, G.G. (1963) A histochemical enzyme kinetic system applied to the trypsin-like amidase and esterase activity in human mast cells. J. Cell Biol. 17, 603-520
    • (1963) J. Cell Biol. , vol.17 , pp. 603-1520
    • Hopsu, V.K.1    Glenner, G.G.2
  • 4
    • 0002079441 scopus 로고
    • Mast cell chymases and tryptases: Phylogeny, family relations and biogenesis
    • Caughey, G.H. (1995) Mast cell chymases and tryptases: Phylogeny, family relations and biogenesis. Clin. Aller. Immunol. 6, 305-329
    • (1995) Clin. Aller. Immunol. , vol.6 , pp. 305-329
    • Caughey, G.H.1
  • 6
    • 0021846232 scopus 로고
    • Chymotrypsin and trypsin-type serine proteases in rat mast cells: Properties and functions
    • Kido, H., Fukusen, N., and Katunuma, N. (1985) Chymotrypsin and trypsin-type serine proteases in rat mast cells: Properties and functions. Arch. Biochem. Biophys. 239, 436-443
    • (1985) Arch. Biochem. Biophys. , vol.239 , pp. 436-443
    • Kido, H.1    Fukusen, N.2    Katunuma, N.3
  • 7
    • 0025772862 scopus 로고
    • Tryptase from rat skin: Purification and properties
    • Braganza, V.J. and Simmons, W.H. (1991) Tryptase from rat skin: Purification and properties. Biochemistry 30, 4997-5007
    • (1991) Biochemistry , vol.30 , pp. 4997-5007
    • Braganza, V.J.1    Simmons, W.H.2
  • 9
    • 0021148042 scopus 로고
    • Human lung tryptase: Purification and characterization
    • Smith, T.J., Hougland, M.W., and Johnson, D.A. (1984) Human lung tryptase: Purification and characterization. J. Biol. Chem. 289, 11046-11051
    • (1984) J. Biol. Chem. , vol.289 , pp. 11046-11051
    • Smith, T.J.1    Hougland, M.W.2    Johnson, D.A.3
  • 11
    • 0015783856 scopus 로고
    • Determination of the amino acid sequence of porcine trypsin by sequenator analysis
    • Hermodson, M.A., Ericsson, L.H., Neurath, H., and Walsh, K.A. (1973) Determination of the amino acid sequence of porcine trypsin by sequenator analysis. Biochemistry 12, 3146-3153
    • (1973) Biochemistry , vol.12 , pp. 3146-3153
    • Hermodson, M.A.1    Ericsson, L.H.2    Neurath, H.3    Walsh, K.A.4
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0022003140 scopus 로고
    • Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase F
    • Tarentino, A.L., Gomez, C.M., and Plummer, T.H., Jr. (1985) Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase F. Biochemistry 24, 4665-4671
    • (1985) Biochemistry , vol.24 , pp. 4665-4671
    • Tarentino, A.L.1    Gomez, C.M.2    Plummer Jr., T.H.3
  • 14
    • 0019423594 scopus 로고
    • Use of the avidinbiotin-peroxidase complex (ABC) in immunoperoxidase techniques
    • Hsu, S.M., Raine, L., and Fanger, H. (1981) Use of the avidinbiotin-peroxidase complex (ABC) in immunoperoxidase techniques. J. Histochem. Cytochem. 29, 577-580
    • (1981) J. Histochem. Cytochem. , vol.29 , pp. 577-580
    • Hsu, S.M.1    Raine, L.2    Fanger, H.3
  • 15
    • 0019492861 scopus 로고
    • A comparative study of the peroxidase-antiperoxidase method and an avidin-biotin complex method for studying polypeptide hormones with radio-immunoassay antibodies
    • Hsu, S.M., Raine, L., and Fanger, H. (1981) A comparative study of the peroxidase-antiperoxidase method and an avidin-biotin complex method for studying polypeptide hormones with radio-immunoassay antibodies. Am. J. Clin. Pathol. 75, 734-738
    • (1981) Am. J. Clin. Pathol. , vol.75 , pp. 734-738
    • Hsu, S.M.1    Raine, L.2    Fanger, H.3
  • 16
    • 0014453665 scopus 로고
    • Proteolytic enzymes in the skin. II. A comparative study of skin homogenates of five mammalian species
    • Jansen, C.T. and Hopsu-Havu, V.K. (1969) Proteolytic enzymes in the skin. II. A comparative study of skin homogenates of five mammalian species. Acta Dermatovenereol. 49, 468-475
    • (1969) Acta Dermatovenereol. , vol.49 , pp. 468-475
    • Jansen, C.T.1    Hopsu-Havu, V.K.2
  • 17
    • 0017874263 scopus 로고
    • Rat skin main neutral protease: Purification and properties
    • Seppä, H.E. and Jarvinen, M. (1978) Rat skin main neutral protease: Purification and properties. J Invest. Dematol. 70, 84-89
    • (1978) J Invest. Dematol. , vol.70 , pp. 84-89
    • Seppä, H.E.1    Jarvinen, M.2
  • 18
    • 0021395620 scopus 로고
    • A simple method for purification of chymase from rat tongue and rat peritoneal cells
    • Kido, H., Fukusen, N., and Katunuma, N. (1984) A simple method for purification of chymase from rat tongue and rat peritoneal cells. Anal. Biochem. 137, 449-453
    • (1984) Anal. Biochem. , vol.137 , pp. 449-453
    • Kido, H.1    Fukusen, N.2    Katunuma, N.3
  • 19
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I. and Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 21
    • 0021044821 scopus 로고
    • Mammalian tissue trypsin-like enzymes: Comparative reactivities of human skin tryptase, human lung tryptase, and bovine trypsin with peptide 4-nitro-anilide and thioester substrates
    • Tanaka, T., McRae, B.J., Cho, K., Cook, R., Fraki, J.E., Johnson, D.A., and Powers, J.C. (1983) Mammalian tissue trypsin-like enzymes: Comparative reactivities of human skin tryptase, human lung tryptase, and bovine trypsin with peptide 4-nitro-anilide and thioester substrates. J. Biol. Chem. 258, 13552-13557
    • (1983) J. Biol. Chem. , vol.258 , pp. 13552-13557
    • Tanaka, T.1    McRae, B.J.2    Cho, K.3    Cook, R.4    Fraki, J.E.5    Johnson, D.A.6    Powers, J.C.7
  • 23
    • 0009551265 scopus 로고
    • Control of tryptase and chymase activity by protease inhibitors
    • Kido, H. and Katunuma, N. (1995) Control of tryptase and chymase activity by protease inhibitors. Clin. Aller. Immunol. 6, 237-256
    • (1995) Clin. Aller. Immunol. , vol.6 , pp. 237-256
    • Kido, H.1    Katunuma, N.2
  • 24
    • 0024434198 scopus 로고
    • Cloning and characterization of complementary cDNA for human tryptase
    • Miller, J.S., Westin, E.H., and Schwartz, L.B. (1989) Cloning and characterization of complementary cDNA for human tryptase. J. Clin. Invest. 84, 1188-1195
    • (1989) J. Clin. Invest. , vol.84 , pp. 1188-1195
    • Miller, J.S.1    Westin, E.H.2    Schwartz, L.B.3
  • 25
    • 0025053169 scopus 로고
    • Cloning and characterization of a second complementary cDNA for human tryptase
    • Miller, J.S., Moxley, G., and Schwartz, L.B. (1990) Cloning and characterization of a second complementary cDNA for human tryptase. J. Clin. Invest. 86, 864-870
    • (1990) J. Clin. Invest. , vol.86 , pp. 864-870
    • Miller, J.S.1    Moxley, G.2    Schwartz, L.B.3
  • 26
    • 0024328773 scopus 로고
    • Molecular cloning of dog mast cell tryptase and a related protease:Structural evidence of a unique mode of serine protease activation
    • Vanderslice, P., Craik, C.S., Nadel, J.A., and Caughey, G.H. (1989) Molecular cloning of dog mast cell tryptase and a related protease:Structural evidence of a unique mode of serine protease activation. Biochemistry 28, 4148-4155
    • (1989) Biochemistry , vol.28 , pp. 4148-4155
    • Vanderslice, P.1    Craik, C.S.2    Nadel, J.A.3    Caughey, G.H.4
  • 27
    • 0025849174 scopus 로고
    • Cloning of the cDNA and gene of mouse mast cell protease 6
    • Reynolds, D.S., Gurley, D.S., Austen, K.F., and Serafin, W.E. (1991) Cloning of the cDNA and gene of mouse mast cell protease 6. J. Biol. Chem. 266, 3847-3853
    • (1991) J. Biol. Chem. , vol.266 , pp. 3847-3853
    • Reynolds, D.S.1    Gurley, D.S.2    Austen, K.F.3    Serafin, W.E.4
  • 29
    • 0029154171 scopus 로고    scopus 로고
    • Cloning of the cDNA encoding mast cell tryptase of Mongolian gerbil, Meriones unguiculatus, and its preferential expression in the intestinal mucosa
    • Murakumo, Y., Ide, H., Itoh, H., Tomita, M., Kobayashi, T., Maruyama, H., Horii, Y., and Nawa, Y. (1996) Cloning of the cDNA encoding mast cell tryptase of Mongolian gerbil, Meriones unguiculatus, and its preferential expression in the intestinal mucosa. Biochem. J. 309, 921-926
    • (1996) Biochem. J. , vol.309 , pp. 921-926
    • Murakumo, Y.1    Ide, H.2    Itoh, H.3    Tomita, M.4    Kobayashi, T.5    Maruyama, H.6    Horii, Y.7    Nawa, Y.8
  • 30
    • 0023644519 scopus 로고
    • Carbohydrate binding properties of complex-type oligosaccharides on immobilized Datura stramonium lectin
    • Yamashita, K., Totani, K., Ohkura, T., Takasaki, S., Goldstein, I.J., and Kobata, A. (1987) Carbohydrate binding properties of complex-type oligosaccharides on immobilized Datura stramonium lectin. J. Biol. Chem. 262, 1602-1607
    • (1987) J. Biol. Chem. , vol.262 , pp. 1602-1607
    • Yamashita, K.1    Totani, K.2    Ohkura, T.3    Takasaki, S.4    Goldstein, I.J.5    Kobata, A.6
  • 31
    • 0021227742 scopus 로고
    • The distribution of repeating [Gal beta 1,4GlcNAc beta 1,3] sequences in asparagine-linked oligosaccharides of the mouse lymphoma cell lines, BW5147 and PHAR 2.1
    • Cummings, R.D. and Kornfeld, S. (1984) The distribution of repeating [Gal beta 1,4GlcNAc beta 1,3] sequences in asparagine-linked oligosaccharides of the mouse lymphoma cell lines, BW5147 and PHAR 2.1. J. Biol. Chem. 259, 6253-6260
    • (1984) J. Biol. Chem. , vol.259 , pp. 6253-6260
    • Cummings, R.D.1    Kornfeld, S.2
  • 32
    • 0019890808 scopus 로고
    • Structural requirements for the binding of oligosaccharides and glycopeptides to immobilized wheat germ agglutinin
    • Yamamoto, K., Tsuji, T., Matsumoto, I., and Osawa, T. (1981) Structural requirements for the binding of oligosaccharides and glycopeptides to immobilized wheat germ agglutinin. Biochemistry 20, 5894-5899
    • (1981) Biochemistry , vol.20 , pp. 5894-5899
    • Yamamoto, K.1    Tsuji, T.2    Matsumoto, I.3    Osawa, T.4
  • 33
    • 0017740540 scopus 로고
    • Isolation and partial characterization of sialoglycopeptides produced by a murine melanoma
    • Bhvanandan, V.P., Umemoto, J., and Davidson, E.A. (1977) Isolation and partial characterization of sialoglycopeptides produced by a murine melanoma. Biochemistry 16, 4426-4437
    • (1977) Biochemistry , vol.16 , pp. 4426-4437
    • Bhvanandan, V.P.1    Umemoto, J.2    Davidson, E.A.3
  • 34
    • 0018387309 scopus 로고
    • The interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid
    • Bhavanandan, V.P. and Katlic, A.W. (1979) The interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid. J. Biol. Chem. 254, 4000-4008
    • (1979) J. Biol. Chem. , vol.254 , pp. 4000-4008
    • Bhavanandan, V.P.1    Katlic, A.W.2
  • 35
  • 36
    • 0016813441 scopus 로고
    • Interaction of immunoglobulin glycopeptides with concanavalin A
    • Kornfeld, R. and Ferris, C. (1975) Interaction of immunoglobulin glycopeptides with concanavalin A. J. Biol. Chem. 250, 2614-2619
    • (1975) J. Biol. Chem. , vol.250 , pp. 2614-2619
    • Kornfeld, R.1    Ferris, C.2
  • 37
    • 0023195836 scopus 로고
    • Use of N-glycanase to release asparagine-linked oligosaccharides for structural analysis
    • Hirani, S., Bernasconi, R.J., and Rasmussen, J.R. (1987) Use of N-glycanase to release asparagine-linked oligosaccharides for structural analysis. Anal. Biochem. 162, 485-492
    • (1987) Anal. Biochem. , vol.162 , pp. 485-492
    • Hirani, S.1    Bernasconi, R.J.2    Rasmussen, J.R.3
  • 39
    • 0022622723 scopus 로고
    • A chymotrypsin-type serine protease in rat basophilic leukemia cells: Evidence for its immunologic identity with atypical mast cell protease
    • Kido, H., Izumi, K., Otsuka, H., Fukusen, N., Kato, Y., and Katunuma, N. (1986) A chymotrypsin-type serine protease in rat basophilic leukemia cells: Evidence for its immunologic identity with atypical mast cell protease. J. Immunol. 138, 1061-1065
    • (1986) J. Immunol. , vol.138 , pp. 1061-1065
    • Kido, H.1    Izumi, K.2    Otsuka, H.3    Fukusen, N.4    Kato, Y.5    Katunuma, N.6
  • 40
    • 0042098660 scopus 로고
    • Mast cell tryptase: Properties and roles in human allergic responses
    • Schwartz, L.B. (1995) Mast cell tryptase: Properties and roles in human allergic responses. Clin. Aller. Immunol. 6, 9-23
    • (1995) Clin. Aller. Immunol. , vol.6 , pp. 9-23
    • Schwartz, L.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.