메뉴 건너뛰기




Volumn 86, Issue 1, 2004, Pages 78-87

Glycoforms of β-Lactoglobulin with Improved Thermostability and Preserved Structural Packing

Author keywords

Lactoglobulin; Glycosylation; Maillard reaction; Monosaccharides; Thermal stability

Indexed keywords

AMINES; GLUCOSE; HYDROPHOBICITY; PROTEINS; THERMODYNAMICS;

EID: 1542615145     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20030     Document Type: Article
Times cited : (86)

References (45)
  • 1
    • 0032825597 scopus 로고    scopus 로고
    • Improvement of heat stability and emulsifying activity of ovalbumin by conjugation with glucuronic acid through the Maillard reaction
    • Aoki T, Hiidome Y, Kitahata K, Sugimoto Y, Ibrahim HR, Kato Y. 1999. Improvement of heat stability and emulsifying activity of ovalbumin by conjugation with glucuronic acid through the Maillard reaction. Food Res Int 32:129-133.
    • (1999) Food Res Int , vol.32 , pp. 129-133
    • Aoki, T.1    Hiidome, Y.2    Kitahata, K.3    Sugimoto, Y.4    Ibrahim, H.R.5    Kato, Y.6
  • 2
    • 78651171852 scopus 로고
    • Improved method for the preparation of crystalline β-lactoglobulin and α-lactalbumin from cow's milk
    • Aschaffenburg R, Drewry J. 1957. Improved method for the preparation of crystalline β-lactoglobulin and α-lactalbumin from cow's milk. Biochem J 65:273-277.
    • (1957) Biochem J , vol.65 , pp. 273-277
    • Aschaffenburg, R.1    Drewry, J.2
  • 3
    • 36949087182 scopus 로고
    • Occurrence of different beta-lactoglobulins in cow's milk
    • Aschaffenburg R, Drewry J. 1955. Occurrence of different beta-lactoglobulins in cow's milk. Nature 176:218-219.
    • (1955) Nature , vol.176 , pp. 218-219
    • Aschaffenburg, R.1    Drewry, J.2
  • 5
    • 0034775565 scopus 로고    scopus 로고
    • Reactions of monosaccharides during heating of sugar-casein systems: Building of a reaction network model
    • Brands CMJ, van Boekel MAJS. 2001. Reactions of monosaccharides during heating of sugar-casein systems: Building of a reaction network model. J Agric Food Chem 49:4667-4675.
    • (2001) J Agric Food Chem , vol.49 , pp. 4667-4675
    • Brands, C.M.J.1    Van Boekel, M.A.J.S.2
  • 7
    • 0011215532 scopus 로고
    • Non-enzymatic browning reactions: Consideration of sugar stability
    • Burton HS, McWeeney DJ. 1963. Non-enzymatic browning reactions: Consideration of sugar stability. Nature 197:266-268.
    • (1963) Nature , vol.197 , pp. 266-268
    • Burton, H.S.1    McWeeney, D.J.2
  • 8
    • 0034921222 scopus 로고    scopus 로고
    • Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar
    • Chevalier F, Chobert J-M, Popineau Y, Nicolas MG, Heartlé T. 2001. Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar. Int Dairy J 11:145-152.
    • (2001) Int Dairy J , vol.11 , pp. 145-152
    • Chevalier, F.1    Chobert, J.-M.2    Popineau, Y.3    Nicolas, M.G.4    Heartlé, T.5
  • 9
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • Chi EY, Krishnan S, Kendrick BS, Chang B, Carpenter JF, Randolph TW. 2003. Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Prot Sci 12:903-913.
    • (2003) Prot Sci , vol.12 , pp. 903-913
    • Chi, E.Y.1    Krishnan, S.2    Kendrick, B.S.3    Chang, B.4    Carpenter, J.F.5    Randolph, T.W.6
  • 10
    • 85022241054 scopus 로고
    • Spectrophotometric assay using o-pthaldialdehyde for determination of proteolysis in milk and isolated milk proteins
    • Church FC, Swaisgood HE, Porter DH, Catignani GL. 1983. Spectrophotometric assay using o-pthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. J Diary Sci 66:1219-1227.
    • (1983) J Diary Sci , vol.66 , pp. 1219-1227
    • Church, F.C.1    Swaisgood, H.E.2    Porter, D.H.3    Catignani, G.L.4
  • 11
    • 0032199307 scopus 로고    scopus 로고
    • Cataract as a conformational disease-the Maillard reaction, alpha-crystallin and chemotherapy
    • Crabbe MJ. 1998. Cataract as a conformational disease-the Maillard reaction, alpha-crystallin and chemotherapy. Cell Mol Biol (Noisy-le-grand) 44:1047-1050.
    • (1998) Cell Mol Biol (Noisy-le-grand) , vol.44 , pp. 1047-1050
    • Crabbe, M.J.1
  • 13
    • 0035290424 scopus 로고    scopus 로고
    • Mild isolation procedure discloses new protein structural properties of beta-lactoglobulin
    • de Jongh HHJ, Gröneveld T, de Groot J. 2001. Mild isolation procedure discloses new protein structural properties of beta-lactoglobulin. J Dairy Sci 84:562-571.
    • (2001) J Dairy Sci , vol.84 , pp. 562-571
    • De Jongh, H.H.J.1    Gröneveld, T.2    De Groot, J.3
  • 14
    • 0028598299 scopus 로고
    • Analysis of circular dichroism spectra of oriented protein-lipid complexes: Toward a general application
    • de Jongh HHJ, Goormaghtigh E, Killian JA. 1994. Analysis of circular dichroism spectra of oriented protein-lipid complexes: Toward a general application. Biochemistry 33:14521-14528.
    • (1994) Biochemistry , vol.33 , pp. 14521-14528
    • De Jongh, H.H.J.1    Goormaghtigh, E.2    Killian, J.A.3
  • 15
    • 0032538350 scopus 로고    scopus 로고
    • Peptide models of local and long-range interactions in the molten globule state of human alpha-lactalbumin
    • Demarest SJ, Fairman R, Raleigh DP. 1998. Peptide models of local and long-range interactions in the molten globule state of human alpha-lactalbumin. J Mol Biol 283:279-291.
    • (1998) J Mol Biol , vol.283 , pp. 279-291
    • Demarest, S.J.1    Fairman, R.2    Raleigh, D.P.3
  • 16
    • 0026440051 scopus 로고
    • Heat-induced aggregation of recombinant erythropoietin in the intact and deglycosylated states as monitored by gel-permeation chromatography combined with a low-angle laser-light scattering technique
    • Endo Y, Nagai H, Watanabe Y, Ochi K, Takagi T. 1992. Heat-induced aggregation of recombinant erythropoietin in the intact and deglycosylated states as monitored by gel-permeation chromatography combined with a low-angle laser-light scattering technique. J Biochem (Tokyo) 112:700-706.
    • (1992) J Biochem (Tokyo) , vol.112 , pp. 700-706
    • Endo, Y.1    Nagai, H.2    Watanabe, Y.3    Ochi, K.4    Takagi, T.5
  • 17
    • 0001675319 scopus 로고
    • Modern aspects of the primary structure and function of β-lactoglobulin
    • Godovac-Zimmermann J, Braunitzer G. 1987. Modern aspects of the primary structure and function of β-lactoglobulin. Milchwissenschaft 42: 294-297.
    • (1987) Milchwissenschaft , vol.42 , pp. 294-297
    • Godovac-Zimmermann, J.1    Braunitzer, G.2
  • 18
    • 0032518864 scopus 로고    scopus 로고
    • Induction of calreticulin expression in response to amino acid deprivation in Chinese hamster ovary cells
    • Heal R, McGivan J. 1998. Induction of calreticulin expression in response to amino acid deprivation in Chinese hamster ovary cells. Biochem J 329:389-394.
    • (1998) Biochem J , vol.329 , pp. 389-394
    • Heal, R.1    McGivan, J.2
  • 19
    • 0033019392 scopus 로고    scopus 로고
    • Alcohol-induced denaturation of beta-lactoglobulin: A close correlation to the alcohol-induced alpha-helix formation of melittin
    • Hirota-Nakaoka N, Goto Y. 1999. Alcohol-induced denaturation of beta-lactoglobulin: A close correlation to the alcohol-induced alpha-helix formation of melittin. Bioorg Med Chem 7:67-73.
    • (1999) Bioorg Med Chem , vol.7 , pp. 67-73
    • Hirota-Nakaoka, N.1    Goto, Y.2
  • 20
    • 0002897822 scopus 로고
    • Improvement of physicochemical and enzymatic-properties of bovine trypsin by nonenzymatic glycation
    • Kato Y, Matsuda T, Nakamura R. 1993. Improvement of physicochemical and enzymatic-properties of bovine trypsin by nonenzymatic glycation. Biosci Biotech Biochem 57:1-5.
    • (1993) Biosci Biotech Biochem , vol.57 , pp. 1-5
    • Kato, Y.1    Matsuda, T.2    Nakamura, R.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T
    • Leammli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Leammli, U.K.1
  • 24
    • 0001139990 scopus 로고
    • Evaluation of kinetic parameters for a glucose-lysine Maillard reaction
    • Lee CM, Sherr B, Koh Y-N. 1984. Evaluation of kinetic parameters for a glucose-lysine Maillard reaction. J. Agric Food Chem 32:379-382.
    • (1984) J Agric Food Chem , vol.32 , pp. 379-382
    • Lee, C.M.1    Sherr, B.2    Koh, Y.-N.3
  • 25
    • 0033992504 scopus 로고    scopus 로고
    • A critical appraisal of the kinetic model for the Maillard browning of glucose with glycine
    • Leong LP, Wedzicha BL. 2000. A critical appraisal of the kinetic model for the Maillard browning of glucose with glycine. Food Chem 68:21-28.
    • (2000) Food Chem , vol.68 , pp. 21-28
    • Leong, L.P.1    Wedzicha, B.L.2
  • 26
    • 1542642943 scopus 로고
    • Antioxidative effect of Maillard reaction products
    • The Swedish Institute for Food and Biotechnology, Göteborg, Sweden
    • Lingnert H. 1979. Antioxidative effect of Maillard reaction products. SIK Rapport no. 458. The Swedish Institute for Food and Biotechnology, Göteborg, Sweden.
    • (1979) SIK Rapport No. 458
    • Lingnert, H.1
  • 27
    • 0017760576 scopus 로고
    • Glycosylation of Escherichia coli L-asparaginase
    • Marsh JW, Denis J Jr., Wriston JC. 1977. Glycosylation of Escherichia coli L-asparaginase. J Biol Chem 252:7678-7684.
    • (1977) J Biol Chem , vol.252 , pp. 7678-7684
    • Marsh, J.W.1    Denis Jr., J.2    Wriston, J.C.3
  • 28
    • 0017252465 scopus 로고
    • Preparation and characterization of a dextran-trypsin conjugate
    • Marshall JJ, Rabinowitz ML. 1976. Preparation and characterization of a dextran-trypsin conjugate. J Biol Chem 251:1081-1087.
    • (1976) J Biol Chem , vol.251 , pp. 1081-1087
    • Marshall, J.J.1    Rabinowitz, M.L.2
  • 29
    • 0027995966 scopus 로고
    • Different effects of N-glycosylation on the thermostability of highly homologous bacterial (1,3-1,4)-beta-glucanases secreted from yeast
    • Meldgaard M, Svendsen I. 1994. Different effects of N-glycosylation on the thermostability of highly homologous bacterial (1,3-1,4)-beta-glucanases secreted from yeast. Microbiology 140:159-166.
    • (1994) Microbiology , vol.140 , pp. 159-166
    • Meldgaard, M.1    Svendsen, I.2
  • 30
    • 0001197838 scopus 로고
    • Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1
    • Montefiori DC, Robinson WE Jr, Mitchell WM. 1988. Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1. Proc Natl Acad Sci USA 85:9248-9250.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 9248-9250
    • Montefiori, D.C.1    Robinson Jr., W.E.2    Mitchell, W.M.3
  • 31
    • 0000774327 scopus 로고    scopus 로고
    • Degradation of tryptophan in heated β-lactoglobulin-lactose mixtures is associated with intense Maillard reaction
    • Moreaux V, Birlouez-Aragon I. 1997. Degradation of tryptophan in heated β-lactoglobulin-lactose mixtures is associated with intense Maillard reaction. J Agric Food Chem 45:1905-1910.
    • (1997) J Agric Food Chem , vol.45 , pp. 1905-1910
    • Moreaux, V.1    Birlouez-Aragon, I.2
  • 32
    • 0345059266 scopus 로고    scopus 로고
    • Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: Effect on association behavior and protein conformation
    • Morgan F, Leonil J, Molle D, Bouhallab S. 1999. Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: Effect on association behavior and protein conformation. J Agric Food Chem 47:83-91.
    • (1999) J Agric Food Chem , vol.47 , pp. 83-91
    • Morgan, F.1    Leonil, J.2    Molle, D.3    Bouhallab, S.4
  • 33
    • 0031577271 scopus 로고    scopus 로고
    • Nonenzymatic lactosylation of bovine β-actoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms
    • Morgan F, Léonil J, Mollé D, Bouhallab S. 1997. Nonenzymatic lactosylation of bovine β-actoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms. Biochem Biophys Res Commun 236:413-417.
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 413-417
    • Morgan, F.1    Léonil, J.2    Mollé, D.3    Bouhallab, S.4
  • 34
    • 0028500948 scopus 로고
    • The preparation and characterization of some amadori compounds (1-amino-1-deoxy-D-fuctose derivatives) derived from a series of aliphatic omega- amino acids
    • Mossine VV, Glinsky GV, Feather MS. 1994. The preparation and characterization of some amadori compounds (1-amino-1-deoxy-D-fuctose derivatives) derived from a series of aliphatic omega- amino acids. Carbohydr Res 262:257-270.
    • (1994) Carbohydr Res , vol.262 , pp. 257-270
    • Mossine, V.V.1    Glinsky, G.V.2    Feather, M.S.3
  • 35
    • 0031026232 scopus 로고    scopus 로고
    • Heat stress induces a glycosylation of membrane sterol in myxoamoebae of a true slime mold, Physarum polycephalum
    • Murakami MK, Nishikawa K, Hirakawa E, Murofushi H. 1997. Heat stress induces a glycosylation of membrane sterol in myxoamoebae of a true slime mold, Physarum polycephalum. J Biol Chem 272:486-489.
    • (1997) J Biol Chem , vol.272 , pp. 486-489
    • Murakami, M.K.1    Nishikawa, K.2    Hirakawa, E.3    Murofushi, H.4
  • 36
    • 0031858644 scopus 로고    scopus 로고
    • Induction of new physicochemical and functional properties by the glycosylation of whey proteins
    • Nacka F, Chobert J-M, Burova T, Léonil J, Haertlé T. 1998. Induction of new physicochemical and functional properties by the glycosylation of whey proteins. J Protein Chem 17:495-503.
    • (1998) J Protein Chem , vol.17 , pp. 495-503
    • Nacka, F.1    Chobert, J.-M.2    Burova, T.3    Léonil, J.4    Haertlé, T.5
  • 39
    • 0000749652 scopus 로고
    • N.M.R. spectroscopy of N-(1-deoxy-D-fructos-1-yl)-L-amino acids ("fructose-amino acids")
    • Röper H, Röper S, Heyns K, Meyer B. 1983. N.M.R. spectroscopy of N-(1-deoxy-D-fructos-1-yl)-L-amino acids ("fructose-amino acids"). Carbohydr Res 116:183-195.
    • (1983) Carbohydr Res , vol.116 , pp. 183-195
    • Röper, H.1    Röper, S.2    Heyns, K.3    Meyer, B.4
  • 41
    • 0029081385 scopus 로고
    • Fructated protein is more resistant to atp-dependent proteolysis than glucated protein possibly as a result of higher content of maillard fluorophores
    • Suárez G, Etlinger DJ, Maturana J, Weitman D. 1995. Fructated protein is more resistant to atp-dependent proteolysis than glucated protein possibly as a result of higher content of maillard fluorophores. Arch Biochem Biophys 321:209-213.
    • (1995) Arch Biochem Biophys , vol.321 , pp. 209-213
    • Suárez, G.1    Etlinger, D.J.2    Maturana, J.3    Weitman, D.4
  • 42
    • 0027967170 scopus 로고
    • The function of heat-shock proteins in stress tolerance
    • Venetianer A, Pirity M, Hever SA. 1994. The function of heat-shock proteins in stress tolerance. Cell Biol Int 18:605-615.
    • (1994) Cell Biol Int , vol.18 , pp. 605-615
    • Venetianer, A.1    Pirity, M.2    Hever, S.A.3
  • 43
    • 0023916019 scopus 로고
    • Identification of a novel stress-inducible glycoprotein in Saccharomyces cerevisiae. I. Preliminary characterization
    • Verma R, Iida H, Pardee AB. 1988. Identification of a novel stress-inducible glycoprotein in Saccharomyces cerevisiae. I. Preliminary characterization. J Biol Chem 263:8569-8575.
    • (1988) J Biol Chem , vol.263 , pp. 8569-8575
    • Verma, R.1    Iida, H.2    Pardee, A.B.3
  • 44
    • 0029904281 scopus 로고    scopus 로고
    • Influence of the carbohydrate moiety on the stability of glycoproteins
    • Wang C, Eufemi M, Turano C, Giartosio A. 1996. Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry 35:7299-7307.
    • (1996) Biochemistry , vol.35 , pp. 7299-7307
    • Wang, C.1    Eufemi, M.2    Turano, C.3    Giartosio, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.