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Volumn 44, Issue 1, 2013, Pages 285-292

Transglutaminase-mediated modification of ovomucoid: Effects on its trypsin inhibitory activity and antigenic properties

Author keywords

Antigenic properties; Monodansylcadaverine; Ovomucoid; Transglutaminase; Trypsin inhibitory activity

Indexed keywords

DANSYLCADAVERINE; OVOMUCOID; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TRYPSIN;

EID: 84871947298     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-011-1155-0     Document Type: Article
Times cited : (32)

References (44)
  • 1
    • 0028322985 scopus 로고
    • Transglutaminases: Protein crosslinking enzymes in tissues and body fluid
    • 7914385 1:CAS:528:DyaK2cXksl2jt7g%3D
    • Aeschlimann D, Paulsson M (1994) Transglutaminases: protein crosslinking enzymes in tissues and body fluid. Thromb Haemost 71(4):402-415
    • (1994) Thromb Haemost , vol.71 , Issue.4 , pp. 402-415
    • Aeschlimann, D.1    Paulsson, M.2
  • 2
    • 0037386736 scopus 로고    scopus 로고
    • A new turn in Rho GTPase activation by Escherichia coli cytotoxic necrotizing factors
    • 12706988 10.1016/S0966-842X(03)00042-8 1:CAS:528:DC%2BD3sXjtFeqtb4%3D
    • Aktories K, Schmidt G (2003) A new turn in Rho GTPase activation by Escherichia coli cytotoxic necrotizing factors. Trends Microbiol 11(4):152-155
    • (2003) Trends Microbiol , vol.11 , Issue.4 , pp. 152-155
    • Aktories, K.1    Schmidt, G.2
  • 3
    • 0024801107 scopus 로고
    • Purification and characteristics of a novel transglutaminase derived from microorganism
    • 10.1271/bbb1961.53.2613 1:CAS:528:DyaK3cXjt1em
    • Ando H, Adachi M, Umeda K, Matsuura A, Nonaka M, Uchio R, Tanaka H, Motoki M (1989) Purification and characteristics of a novel transglutaminase derived from microorganism. Agric Biol Chem 53:2613-2617
    • (1989) Agric Biol Chem , vol.53 , pp. 2613-2617
    • Ando, H.1    Adachi, M.2    Umeda, K.3    Matsuura, A.4    Nonaka, M.5    Uchio, R.6    Tanaka, H.7    Motoki, M.8
  • 4
    • 0000016467 scopus 로고    scopus 로고
    • Effect of polysaccharide conjugation or transglutaminase treatment on the allergenicity and functional properties of soy protein
    • 10.1021/jf9705072
    • Babiker EE, Hiroyuki A, Matsudomi N, Iwata H, Ogawa T, Bando N, Kato A (1998) Effect of polysaccharide conjugation or transglutaminase treatment on the allergenicity and functional properties of soy protein. J Agric Food Chem 46:566-571
    • (1998) J Agric Food Chem , vol.46 , pp. 566-571
    • Babiker, E.E.1    Hiroyuki, A.2    Matsudomi, N.3    Iwata, H.4    Ogawa, T.5    Bando, N.6    Kato, A.7
  • 5
    • 0028276761 scopus 로고
    • Allergenicity and antigenicity of chicken egg ovomucoid (Gal d III) compared with ovalbumin (Gal d I) in children with egg allergy and in mice
    • 8006309 10.1016/S0091-6749(94)70054-0 1:CAS:528:DyaK2MXptlaksL0%3D
    • Bernhisel-Broadbent J, Dintzis HM, Dintzis RZ, Sampson HA (1994) Allergenicity and antigenicity of chicken egg ovomucoid (Gal d III) compared with ovalbumin (Gal d I) in children with egg allergy and in mice. J Allergy Clin Immunol 93:1047-1059
    • (1994) J Allergy Clin Immunol , vol.93 , pp. 1047-1059
    • Bernhisel-Broadbent, J.1    Dintzis, H.M.2    Dintzis, R.Z.3    Sampson, H.A.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 942051 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
    • Bradford M (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 7
    • 84987277329 scopus 로고
    • In vitro enzymatic hydrolysis of phaseolin, the major storage protein of Phaseolus vulgaris L
    • 10.1111/j.1365-2621.1987.tb14074.x 1:CAS:528:DyaL1cXptVSmug%3D%3D
    • Deshpande SS, Nielsen SS (1987) In vitro enzymatic hydrolysis of phaseolin, the major storage protein of Phaseolus vulgaris L. J Food Sci 52:1326-1329
    • (1987) J Food Sci , vol.52 , pp. 1326-1329
    • Deshpande, S.S.1    Nielsen, S.S.2
  • 8
    • 4544369373 scopus 로고
    • The specificities of chicken ovomucoid and ovoinhibitor
    • 13944692 1:CAS:528:DyaF3sXmtV2lsQ%3D%3D
    • Feeney R, Stevens F, Osuga D (1963) The specificities of chicken ovomucoid and ovoinhibitor. J Biol Chem 238:1415-1418
    • (1963) J Biol Chem , vol.238 , pp. 1415-1418
    • Feeney, R.1    Stevens, F.2    Osuga, D.3
  • 9
    • 0022272467 scopus 로고
    • Transglutaminases
    • 10.1016/S0076-6879(85)13049-1
    • Folk JE, Chung SI (1985) Transglutaminases. Methods Enzymol 11:358-364
    • (1985) Methods Enzymol , vol.11 , pp. 358-364
    • Folk, J.E.1    Chung, S.I.2
  • 10
    • 0017680149 scopus 로고
    • The epsilon-(gamma-glutamyl)lysine cross-link and the catalytic role of the transglutaminases
    • 10.1016/S0065-3233(08)60217-X 1:CAS:528:DyaE1cXksFGhtr0%3D
    • Folk JE, Finlayson JS (1977) The epsilon-(gamma-glutamyl)lysine cross-link and the catalytic role of the transglutaminases. Adv Prot Chem 31:1-133
    • (1977) Adv Prot Chem , vol.31 , pp. 1-133
    • Folk, J.E.1    Finlayson, J.S.2
  • 11
    • 0038951369 scopus 로고
    • Essential groups for the interaction of ovomucoid (egg white trypsin inhibitor) and trypsin, and for tryptic activity
    • 18107443 1:CAS:528:DyaH1MXjvFeruw%3D%3D
    • Fraenkel-Conrat H, Bean RS, Lineweaver HJ (1949) Essential groups for the interaction of ovomucoid (egg white trypsin inhibitor) and trypsin, and for tryptic activity. J Biol Chem 177:385-403
    • (1949) J Biol Chem , vol.177 , pp. 385-403
    • Fraenkel-Conrat, H.1    Bean, R.S.2    Lineweaver, H.J.3
  • 12
    • 0000068631 scopus 로고    scopus 로고
    • Glycation of proteinous inhibitors: Loss in trypsin inhibitory activity by the blocking of arginine and lysine residues at their reactive sites
    • 10.1021/jf970310+ 1:CAS:528:DyaK2sXmtlKkur8%3D
    • Kato Y, Matsuda T (1997) Glycation of proteinous inhibitors: loss in trypsin inhibitory activity by the blocking of arginine and lysine residues at their reactive sites. J Agric Food Chem 45:3826-3831
    • (1997) J Agric Food Chem , vol.45 , pp. 3826-3831
    • Kato, Y.1    Matsuda, T.2
  • 13
    • 0001109729 scopus 로고
    • Formation of intermolecular beta-sheet structure during heat denaturation of ovoalbumin
    • 10.1021/jf00084a007 1:CAS:528:DyaL1cXlvVyqsbY%3D
    • Kato A, Takagi T (1988) Formation of intermolecular beta-sheet structure during heat denaturation of ovoalbumin. J Agric Food Chem 36:1156-1159
    • (1988) J Agric Food Chem , vol.36 , pp. 1156-1159
    • Kato, A.1    Takagi, T.2
  • 14
    • 0023129864 scopus 로고
    • Chicken ovomucoid: Determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all three of its domains
    • 3548816 10.1021/bi00375a027 1:CAS:528:DyaL2sXks1altA%3D%3D
    • Kato I, Schrode J, Kohr W, Laskowski M (1987) Chicken ovomucoid: determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all three of its domains. Biochemistry 26:193-201
    • (1987) Biochemistry , vol.26 , pp. 193-201
    • Kato, I.1    Schrode, J.2    Kohr, W.3    Laskowski, M.4
  • 15
    • 0032744507 scopus 로고    scopus 로고
    • Effects of amino acid replacements around the reactive site of chicken ovomucoid domain 3 on the inhibitory activity toward chymotrypsin and trypsin
    • Kojima S, Takagi N, Minagawa T, Fushimi N, Miura K-I (1999) Effects of amino acid replacements around the reactive site of chicken ovomucoid domain 3 on the inhibitory activity toward chymotrypsin and trypsin. Prot Eng 10:857-862
    • (1999) Prot Eng , vol.10 , pp. 857-862
    • Kojima, S.1    Takagi, N.2    Minagawa, T.3    Fushimi, N.4    Miura, K.-I.5
  • 16
    • 0001456780 scopus 로고
    • Studies on the allergenic structure of hen ovomucoid by chemical and enzymic fragmentation
    • 10.1271/bbb1961.45.879 1:CAS:528:DyaL3MXhvFSisbY%3D
    • Kurisaki J, Konishi Y, Kaminogawa S, Yamauchi K (1981) Studies on the allergenic structure of hen ovomucoid by chemical and enzymic fragmentation. Agric Biol Chem 45:879-886
    • (1981) Agric Biol Chem , vol.45 , pp. 879-886
    • Kurisaki, J.1    Konishi, Y.2    Kaminogawa, S.3    Yamauchi, K.4
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 5432063 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli UK (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
  • 18
    • 0019984788 scopus 로고
    • A clinical and immunological study of allergy to hen's egg white. II. Antigens in hen's egg white studied by crossed immunoelectrophoresis (CIE)
    • 7125151 10.1111/j.1398-9995.1982.tb01918.x 1:CAS:528:DyaL38XlsVarsL0%3D
    • Langeland T (1982) A clinical and immunological study of allergy to hen's egg white. II. Antigens in hen's egg white studied by crossed immunoelectrophoresis (CIE). Allergy 37(5):323-333
    • (1982) Allergy , vol.37 , Issue.5 , pp. 323-333
    • Langeland, T.1
  • 19
    • 0000371853 scopus 로고    scopus 로고
    • Transglutaminase cross-linked egg white protein films: Tensile properties and oxygen permeability
    • 10.1021/jf980567n 1:CAS:528:DyaK1cXmtFarsbs%3D
    • Lim L-T, Mine Y, Tung MA (1998) Transglutaminase cross-linked egg white protein films: tensile properties and oxygen permeability. J Agric Food Chem 46:4022-4029
    • (1998) J Agric Food Chem , vol.46 , pp. 4022-4029
    • Lim, L.-T.1    Mine, Y.2    Tung, M.A.3
  • 20
    • 0001626519 scopus 로고
    • Identification of the trypsin inhibitor of egg white with ovomucoid
    • 20272096 1:CAS:528:DyaH1cXovVyl
    • Lineweaver H, Murray CW (1947) Identification of the trypsin inhibitor of egg white with ovomucoid. J Biol Chem 171:565-581
    • (1947) J Biol Chem , vol.171 , pp. 565-581
    • Lineweaver, H.1    Murray, C.W.2
  • 21
    • 78650999898 scopus 로고
    • Determination of trypsin in the presence of egg white trypsin inhibitor and demonstration of absence of trypsin from egg white
    • 18107424 1:CAS:528:DyaH1MXjs1yksQ%3D%3D
    • Lineweaver H, Fraenkel-Conrat H, Bean RS (1949) Determination of trypsin in the presence of egg white trypsin inhibitor and demonstration of absence of trypsin from egg white. J Biol Chem 177:205-207
    • (1949) J Biol Chem , vol.177 , pp. 205-207
    • Lineweaver, H.1    Fraenkel-Conrat, H.2    Bean, R.S.3
  • 22
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • 12563291 10.1038/nrm1014 1:CAS:528:DC%2BD3sXnsFaqtg%3D%3D
    • Lorand L, Graham RM (2003) Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol 4:140-156
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 23
    • 34250742375 scopus 로고    scopus 로고
    • Synthesis and resistance to in vitro proteolysis of transglutaminase- crosslinked phaseolin, the major storage protein from Phaseolus vulgaris
    • 17516654 10.1021/jf0637269 1:CAS:528:DC%2BD2sXls1SmtLo%3D
    • Mariniello L, Giosafatto CVL, Di Pierro P, Sorrentino A, Porta R (2007a) Synthesis and resistance to in vitro proteolysis of transglutaminase-crosslinked phaseolin, the major storage protein from Phaseolus vulgaris. J Agric Food Chem 55:4717-4721
    • (2007) J Agric Food Chem , vol.55 , pp. 4717-4721
    • Mariniello, L.1    Giosafatto, C.V.L.2    Di Pierro, P.3    Sorrentino, A.4    Porta, R.5
  • 25
    • 77956540423 scopus 로고    scopus 로고
    • Transglutaminase in food biotechnology
    • R. Porta L. Mariniello Di Pierro (eds) enzymes as additives or processing aids. Research Signpost Trivandum Kerala
    • Mariniello L, Di Pierro P, Giosafatto CVL, Sorrentino A, Porta R (2008) Transglutaminase in food biotechnology. In: Porta R, Mariniello L, Di Pierro P (eds) Recent developments in food biotechnology. enzymes as additives or processing aids. Research Signpost Trivandum, Kerala, pp 185-211
    • (2008) Recent Developments in Food Biotechnology , pp. 185-211
    • Mariniello, L.1    Di Pierro, P.2    Giosafatto, C.V.L.3    Sorrentino, A.4    Porta, R.5
  • 26
    • 0020488920 scopus 로고
    • The secondary structure of ovomucoid and its domains as studied by circular dichroism
    • 6182916 10.1016/0167-4838(82)90404-6 1:CAS:528:DyaL38XlvFCktLs%3D
    • Matsuda T, Watanabe K, Nakamura R (1982) The secondary structure of ovomucoid and its domains as studied by circular dichroism. Biochim Biophys Acta 707:121-128
    • (1982) Biochim Biophys Acta , vol.707 , pp. 121-128
    • Matsuda, T.1    Watanabe, K.2    Nakamura, R.3
  • 27
    • 84987288583 scopus 로고
    • Immunoreactive glycopeptides separated from peptic hydrolysate of chicken egg white ovomucoid
    • 10.1111/j.1365-2621.1985.tb13751.x 1:CAS:528:DyaL2MXktVGisbo%3D
    • Matsuda T, Gu J, Tsuruta K, Nakamura R (1985) Immunoreactive glycopeptides separated from peptic hydrolysate of chicken egg white ovomucoid. J Food Sci 50:592-594
    • (1985) J Food Sci , vol.50 , pp. 592-594
    • Matsuda, T.1    Gu, J.2    Tsuruta, K.3    Nakamura, R.4
  • 28
    • 0030044861 scopus 로고    scopus 로고
    • Enhanced susceptibility to transglutaminase reaction of α-lactalbumin in the molten globule state
    • 8547351 10.1016/0167-4838(95)00197-2
    • Matsumura Y, Chanyongvorakul Y, Kumazawa Y, Ohtsuka T, Mori T (1996) Enhanced susceptibility to transglutaminase reaction of α-lactalbumin in the molten globule state. Biochim Biophys Acta 1292:69-76
    • (1996) Biochim Biophys Acta , vol.1292 , pp. 69-76
    • Matsumura, Y.1    Chanyongvorakul, Y.2    Kumazawa, Y.3    Ohtsuka, T.4    Mori, T.5
  • 29
    • 0036288997 scopus 로고    scopus 로고
    • Identification and fine mapping of IgG and IgE epitopes in ovomucoid
    • 11944924 10.1006/bbrc.2002.6725 1:CAS:528:DC%2BD38Xis1ygt70%3D
    • Mine Y, Wei Zhang J (2002) Identification and fine mapping of IgG and IgE epitopes in ovomucoid. Biochem Biophys Res Commun 292:1070-1074
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 1070-1074
    • Mine, Y.1    Wei Zhang, J.2
  • 30
    • 0002976987 scopus 로고
    • Thermally induced changes in egg white proteins
    • 10.1021/jf00102a004 1:CAS:528:DyaK3cXmt12rsLY%3D
    • Mine Y, Noutomi T, Haga N (1990) Thermally induced changes in egg white proteins. J Agric Food Chem 38:2122-2125
    • (1990) J Agric Food Chem , vol.38 , pp. 2122-2125
    • Mine, Y.1    Noutomi, T.2    Haga, N.3
  • 31
    • 78651124680 scopus 로고
    • The carbohydrate of ovomucoid. Isolation of glycopeptides and the carbohydrate-protein linkage
    • 14109185 1:CAS:528:DyaF3sXks1emsr8%3D
    • Montgomery R, Wu YC (1963) The carbohydrate of ovomucoid. Isolation of glycopeptides and the carbohydrate-protein linkage. J Biol Chem 238:3547-3554
    • (1963) J Biol Chem , vol.238 , pp. 3547-3554
    • Montgomery, R.1    Wu, Y.C.2
  • 33
    • 0033587684 scopus 로고    scopus 로고
    • A novel function for transglutaminase 1: Attachment of long-chain omega-hydroxyceramides to involucrin by ester bond formation
    • 10411887 10.1073/pnas.96.15.8402 1:CAS:528:DyaK1MXkslOks7Y%3D
    • Nemes Z, Marekov LN, Fesus L, Steinert PM (1999) A novel function for transglutaminase 1: attachment of long-chain omega-hydroxyceramides to involucrin by ester bond formation. Proc Natl Acad Sci 96(15):8402-8407
    • (1999) Proc Natl Acad Sci , vol.96 , Issue.15 , pp. 8402-8407
    • Nemes, Z.1    Marekov, L.N.2    Fesus, L.3    Steinert, P.M.4
  • 36
    • 33644631475 scopus 로고    scopus 로고
    • Engineered recombinant ovomucoid third domain can modulate allergenic response in Balb/c mice model
    • 16494843 10.1016/j.bbrc.2006.01.174 1:CAS:528:DC%2BD28XitVKjsbw%3D
    • Rupa P, Mine Y (2006) Engineered recombinant ovomucoid third domain can modulate allergenic response in Balb/c mice model. Biochem Biophys Res Com 342:710-717
    • (2006) Biochem Biophys Res Com , vol.342 , pp. 710-717
    • Rupa, P.1    Mine, Y.2
  • 37
    • 0030990950 scopus 로고    scopus 로고
    • Effects of sodium chloride, phytate and tannin on in vitro proteolysis of phaseolin
    • 10.1016/S0308-8146(96)00258-0 1:CAS:528:DyaK2sXitl2js70%3D
    • Sathe SK, Sze-tao KWC (1997) Effects of sodium chloride, phytate and tannin on in vitro proteolysis of phaseolin. Food Chem 59:253-259
    • (1997) Food Chem , vol.59 , pp. 253-259
    • Sathe, S.K.1    Sze-Tao, K.W.C.2
  • 39
    • 0016480053 scopus 로고
    • Solubility characteristics of globulins from Phaseolus seeds in regard to their isolation and characterization
    • 10.1021/jf60198a004
    • Sun S, Hall T (1975) Solubility characteristics of globulins from Phaseolus seeds in regard to their isolation and characterization. J Agric Food Chem 23:1984-1989
    • (1975) J Agric Food Chem , vol.23 , pp. 1984-1989
    • Sun, S.1    Hall, T.2
  • 40
    • 0034278161 scopus 로고    scopus 로고
    • Producing a low ovomucoid egg white preparation with aqueous ethanol
    • 11055414 10.1271/bbb.64.2005 1:CAS:528:DC%2BD3cXnt1arurY%3D
    • Tanabe S, Tesaki S, Watanabe M (2000) Producing a low ovomucoid egg white preparation with aqueous ethanol. Biosci Biotechnol Biochem 64:2005-2007
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 2005-2007
    • Tanabe, S.1    Tesaki, S.2    Watanabe, M.3
  • 42
    • 85008124098 scopus 로고
    • Controlled enzymatic treatment of wheat proteins for producing of hypoallergenic flour
    • 10.1271/bbb.58.388 1:CAS:528:DyaK2cXitFGks78%3D
    • Watanabe M, Suzuki T, Ikenzawa Z, Arai S (1994) Controlled enzymatic treatment of wheat proteins for producing of hypoallergenic flour. Biosci Biotechnol Biochem 58:388-390
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 388-390
    • Watanabe, M.1    Suzuki, T.2    Ikenzawa, Z.3    Arai, S.4
  • 43
    • 0036901776 scopus 로고    scopus 로고
    • Visualization of chicken ovomucoid in polyacrylamide gels
    • 12441160 10.1016/S0003-2697(02)00385-8 1:CAS:528:DC%2BD38Xos1GntLk%3D
    • Yousif AN, Kan JW (2002) Visualization of chicken ovomucoid in polyacrylamide gels. Anal Biochem 311:93-97
    • (2002) Anal Biochem , vol.311 , pp. 93-97
    • Yousif, A.N.1    Kan, J.W.2
  • 44
    • 0041767546 scopus 로고    scopus 로고
    • Transglutaminase from Streptomyces mobaraensis is activated by an endogenous metalloprotease
    • 12869197 10.1046/j.1432-1033.2003.03703.x 1:CAS:528:DC%2BD3sXmt1Skt78%3D
    • Zotzel J, Keller P, Fuchsbauer H-L (2003) Transglutaminase from Streptomyces mobaraensis is activated by an endogenous metalloprotease. Eur J Biochem 270:3214-3222
    • (2003) Eur J Biochem , vol.270 , pp. 3214-3222
    • Zotzel, J.1    Keller, P.2    Fuchsbauer, H.-L.3


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