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Volumn 15, Issue 1, 2004, Pages 27-34

Effect of Limited Solid-State Glycation on the Conformation of Lysozyme by ESI-MSMS Peptide Mapping and Molecular Modeling

Author keywords

[No Author keywords available]

Indexed keywords

CHROMATOGRAPHY; ENZYMES; MAPPING; MOLECULAR MODELING; PEPTIDES;

EID: 0842328432     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc034083v     Document Type: Article
Times cited : (44)

References (34)
  • 1
    • 0029763759 scopus 로고    scopus 로고
    • Role of Maillard reaction in diabetes mellitus and diseases of aging
    • Thorpe, S. R., and Baynes, J. W. (1996) Role of Maillard reaction in diabetes mellitus and diseases of aging. Drugs Aging 9, 69-77.
    • (1996) Drugs Aging , vol.9 , pp. 69-77
    • Thorpe, S.R.1    Baynes, J.W.2
  • 2
    • 0033049779 scopus 로고    scopus 로고
    • Advanced glycation end-products in diabetes nephropathy
    • Friedman, E. A. (1999) Advanced glycation end-products in diabetes nephropathy. Nephrol. Dial. Transplant.. 14 (Suppl. 3), 1-9.
    • (1999) Nephrol. Dial. Transplant. , vol.14 , Issue.SUPPL. 3 , pp. 1-9
    • Friedman, E.A.1
  • 3
    • 0029118168 scopus 로고
    • Formation of immunochemical advanced glycosylation end products precedes and correlates with early manifestations of renal and retinal disease in diabetes
    • Beisswenger, P. J., Makita, Z., Curphey, T. J., Moore, L. L., Jean, S., Brinck-Johnsen, T., Bucala, R., and Vlassara, H. (1995) Formation of immunochemical advanced glycosylation end products precedes and correlates with early manifestations of renal and retinal disease in diabetes. Diabetes 44 (7), 824-9.
    • (1995) Diabetes , vol.44 , Issue.7 , pp. 824-829
    • Beisswenger, P.J.1    Makita, Z.2    Curphey, T.J.3    Moore, L.L.4    Jean, S.5    Brinck-Johnsen, T.6    Bucala, R.7    Vlassara, H.8
  • 4
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee, M. (2001) Biochemistry and molecular cell biology of diabetic complications. Nature 414 (6865), 813-20.
    • (2001) Nature , vol.414 , Issue.6865 , pp. 813-820
    • Brownlee, M.1
  • 5
    • 0034294932 scopus 로고    scopus 로고
    • Glycation as the glucose link to diabetic complications
    • Gugliucci, A. (2000) Glycation as the glucose link to diabetic complications. Clin Prac. 100, 621-634.
    • (2000) Clin Prac , vol.100 , pp. 621-634
    • Gugliucci, A.1
  • 6
    • 0001754056 scopus 로고    scopus 로고
    • Preparation of neoglycoprotein from carp myofibrillar protein by Maillard reaction with glucose: Biochemical properties and emulsifying properties
    • Saeki, H. (1997) Preparation of neoglycoprotein from carp myofibrillar protein by Maillard reaction with glucose: biochemical properties and emulsifying properties. J. Agric. Food Chem. 45, 680-684.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 680-684
    • Saeki, H.1
  • 7
    • 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., Leonil, J., Haertle, 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    Leonil, J.4    Haertle, T.5
  • 8
    • 1542576759 scopus 로고    scopus 로고
    • Some physicochemical properties and structural changes of bovine beta-casein upon glycation
    • Darewicz, M., Dziuba, J., Mioduszewska, H. (1998) Some physicochemical properties and structural changes of bovine beta-casein upon glycation. Nahrung 42 (3-4), 213-214.
    • (1998) Nahrung , vol.42 , Issue.3-4 , pp. 213-214
    • Darewicz, M.1    Dziuba, J.2    Mioduszewska, H.3
  • 9
    • 84986492825 scopus 로고
    • Emulsion stabilization by Maillard-type covalent complex of plasma protein with galactomannan
    • Matsumodi, N., Inoue, Y., Nakashima, H., Kato, A., Kobayashi, K. (1995) Emulsion stabilization by Maillard-type covalent complex of plasma protein with galactomannan. J. Food Sci. 60, 265-268, 283.
    • (1995) J. Food Sci. , vol.60 , pp. 265-268
    • Matsumodi, N.1    Inoue, Y.2    Nakashima, H.3    Kato, A.4    Kobayashi, K.5
  • 10
    • 0000204035 scopus 로고    scopus 로고
    • Effects of the length of polysaccharide chains on the functional properties of the Maillard-type lysozyme -polysaccharide conjugate
    • Shu, Y. W., Sahara, S., Nakamura, S., and Kato, A. (1996) Effects of the length of polysaccharide chains on the functional properties of the Maillard-type lysozyme -polysaccharide conjugate. J. Agric. Food Chem. 44, 2544-2548.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 2544-2548
    • Shu, Y.W.1    Sahara, S.2    Nakamura, S.3    Kato, A.4
  • 11
    • 0032822981 scopus 로고    scopus 로고
    • Functional improvement in dried egg white through the Maillard reaction
    • Handa, A., and Kuroda, N. (1999) Functional improvement in dried egg white through the Maillard reaction. J. Agric. Food Chem. 47, 1845-1850.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 1845-1850
    • Handa, A.1    Kuroda, N.2
  • 12
    • 21344456480 scopus 로고    scopus 로고
    • Bovine serum albumin gelation as a result of the Maillard reaction
    • Mat Easa, A., Hill, S. E., Mitchell, J. R., and Taylor, A. J. (1996) Bovine serum albumin gelation as a result of the Maillard reaction. Food Hydrocoll. 10, 199-202.
    • (1996) Food Hydrocoll. , vol.10 , pp. 199-202
    • Mat Easa, A.1    Hill, S.E.2    Mitchell, J.R.3    Taylor, A.J.4
  • 13
    • 0542392034 scopus 로고    scopus 로고
    • Novel functional properties of glycosylated lysozyme constructed by chemical and genetic modifications
    • (Parris, N., Kato, A., Creamer, L., and Pearce, J., Eds.), ACS Symposium Series 650, American Chemical Society: Washington, DC
    • Kato, A., Nakamura, S., Takasaki, H., and Maki, S. (1996) Novel functional properties of glycosylated lysozyme constructed by chemical and genetic modifications. Macromolecular Interactions in Food Technology (Parris, N., Kato, A., Creamer, L., and Pearce, J., Eds.) pp 242-256, ACS Symposium Series 650, American Chemical Society: Washington, DC.
    • (1996) Macromolecular Interactions in Food Technology , pp. 242-256
    • Kato, A.1    Nakamura, S.2    Takasaki, H.3    Maki, S.4
  • 14
    • 33751500314 scopus 로고
    • New antimicrobial characteristics of lysozyme-dextran conjugate
    • Nakamura, S., Kato, A., and Kobayashi, K. (1991) New antimicrobial characteristics of lysozyme-dextran conjugate. J. Agric. Food Chem. 39, 647-650.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 647-650
    • Nakamura, S.1    Kato, A.2    Kobayashi, K.3
  • 15
    • 0002897822 scopus 로고
    • Improvement of physicochemical and enzymatic properties of bovine trypsin by non-enzymatic glycation
    • Kato, Y., Matsuda, T., and Nakamura, R. (1993) Improvement of physicochemical and enzymatic properties of bovine trypsin by non-enzymatic glycation. Biosci. Biotechnol. Biochem. 57, 1-5.
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1-5
    • Kato, Y.1    Matsuda, T.2    Nakamura, R.3
  • 16
    • 0345059266 scopus 로고    scopus 로고
    • Modification of bovine □-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., and Bouhallab, S. (1999) Modification of bovine □-lactoglobulin by glycation in a powdered state or in an aqueous solution: Effect on association behavior and protein conformation. J. Agric. Food Chem. 47 (1), 83-91.
    • (1999) J. Agric. Food Chem. , vol.47 , Issue.1 , pp. 83-91
    • Morgan, F.1    Leonil, J.2    Molle, D.3    Bouhallab, S.4
  • 17
    • 0034921222 scopus 로고    scopus 로고
    • Improvement of the functional properties of xe2β-lactoglobulin glycated through the Maillard reaction is related to the sugar nature
    • Chevalier, F., Chobert, J., M.; Popineau, Y., Nicolas, M. G., and Haertle, T. (2001) Improvement of the functional properties of xe2β-lactoglobulin glycated through the Maillard reaction is related to the sugar nature. 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    Haertle, T.5
  • 18
    • 0025239329 scopus 로고
    • In vitro non-enzymatic glycation and formation of browning products in the bovine lens alpha-crystallin
    • Liang, J. N., Rossi, M. T. (1990) In vitro non-enzymatic glycation and formation of browning products in the bovine lens alpha-crystallin. Exp. Eye Res. 50 (4), 367-371.
    • (1990) Exp. Eye Res. , vol.50 , Issue.4 , pp. 367-371
    • Liang, J.N.1    Rossi, M.T.2
  • 19
    • 0027321526 scopus 로고
    • Inhibitory effect of nonenzymatic glycation on ubiquitination and ubiquitin-mediated degradation of lysozyme
    • Takizawa, N., Takada, K., and Ohkawa, K. (1993) Inhibitory effect of nonenzymatic glycation on ubiquitination and ubiquitin-mediated degradation of lysozyme. Biochem. Biophys. Res. Commun. 192 (2), 700-706.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , Issue.2 , pp. 700-706
    • Takizawa, N.1    Takada, K.2    Ohkawa, K.3
  • 20
    • 0029777555 scopus 로고    scopus 로고
    • Interactions of elastin and aorta with sugars in vitro and their effect on biochemical and physical properties
    • Winlove, C. P., Parler, K. H., Avery, N. C., and Bailey, A.J. (1996) Interactions of elastin and aorta with sugars in vitro and their effect on biochemical and physical properties. Diabetologia 39 (10), 1131-1139.
    • (1996) Diabetologia , vol.39 , Issue.10 , pp. 1131-1139
    • Winlove, C.P.1    Parler, K.H.2    Avery, N.C.3    Bailey, A.J.4
  • 22
    • 0037168275 scopus 로고    scopus 로고
    • Integrity of crystalline lysozyme exceeds that of a spray-dried form
    • Elkordy, A. A., Forbes, R. T., and Barry, B. W. (2002) Integrity of crystalline lysozyme exceeds that of a spray-dried form. Int. J. Pharm. 247 (1-2), 79-90.
    • (2002) Int. J. Pharm. , vol.247 , Issue.1-2 , pp. 79-90
    • Elkordy, A.A.1    Forbes, R.T.2    Barry, B.W.3
  • 23
    • 0035375318 scopus 로고    scopus 로고
    • Analysis of glycated proteins by mass spectrometric techniques: Qualitative and quantitative aspects
    • Yeboah, F. K., and Yaylayan, V. A. (2001) Analysis of glycated proteins by mass spectrometric techniques: qualitative and quantitative aspects. Nahrung/Food. 45 (3), 64-171.
    • (2001) Nahrung/Food , vol.45 , Issue.3 , pp. 64-171
    • Yeboah, F.K.1    Yaylayan, V.A.2
  • 24
    • 0032540692 scopus 로고    scopus 로고
    • Use of Locally Enhanced Sampling in Free Energy Calculations: Testing and Application to the α to β Anomerization of Glucose
    • Simmering, C., Fox, T., and Kollman, P. A. (1998) Use of Locally Enhanced Sampling in Free Energy Calculations: Testing and Application to the α to β Anomerization of Glucose. J. Am. Chem. Soc. 120, 5772-5782.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5772-5782
    • Simmering, C.1    Fox, T.2    Kollman, P.A.3
  • 25
    • 0029011701 scopus 로고
    • A Second Generation Force Field for the Simulation of Proteins. Nucleic acids and Organic Molecules
    • Cornell, W. D. (1995) A Second Generation Force Field for the Simulation of Proteins, Nucleic acids and Organic Molecules. J. Am. Chem. Soc. 117, 5179-5197.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1
  • 27
    • 0000667030 scopus 로고
    • Application of RESP Charges to Calculate Conformational Energies. Hydrogen Bond Energies, and Free Energies of Solvation
    • Cornell, W. D., Cieplak, P., Bayly, C. I., and Kollman, P. A. (1993) Application of RESP Charges to Calculate Conformational Energies, Hydrogen Bond Energies, and Free Energies of Solvation. J. Am. Chem. Soc., 115, 9620-9631.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 9620-9631
    • Cornell, W.D.1    Cieplak, P.2    Bayly, C.I.3    Kollman, P.A.4
  • 29
    • 84986456126 scopus 로고
    • A Simple Yet Accurate Boundary Element Method for Continuum Dielectric Calculations
    • Purisima, E. O., and Nilar, S. H. (1995) A Simple Yet Accurate Boundary Element Method for Continuum Dielectric Calculations. J. Comput. Chem. 16 (6), 681-689.
    • (1995) J. Comput. Chem. , vol.16 , Issue.6 , pp. 681-689
    • Purisima, E.O.1    Nilar, S.H.2
  • 30
    • 0005652597 scopus 로고    scopus 로고
    • First Summation Boundary Element Method for Calculating Solvation Free Energies of Macromolecules
    • Purisima, E. O. (1998) First Summation Boundary Element Method for Calculating Solvation Free Energies of Macromolecules. J. Comput. Chem. 19 (13), 1494-1505.
    • (1998) J. Comput. Chem. , vol.19 , Issue.13 , pp. 1494-1505
    • Purisima, E.O.1
  • 31
    • 0023430366 scopus 로고
    • Monte Carlo Minimization Approach to the Multiple-Minima Problem in Protein Folding
    • Li, Z., and Scheraga, H. A. (1987) Monte Carlo Minimization Approach to the Multiple-Minima Problem in Protein Folding. Proc. Natl. Acad. Sci. U.S.A. 84, 6611-6615.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 6611-6615
    • Li, Z.1    Scheraga, H.A.2
  • 33
    • 0026625689 scopus 로고
    • Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping
    • Suckau, D., Mak, M., and Przybylski, M. (1992) Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping. Proc Natl Acad Sci. U.S.A. 89 (12), 5630-5634.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , Issue.12 , pp. 5630-5634
    • Suckau, D.1    Mak, M.2    Przybylski, M.3
  • 34
    • 0027482860 scopus 로고
    • Structural consequences of reductive methylation of lysine residues in hen egg white lysozyme: An X-ray analysis at 1.8-A resolution
    • Rypniewski, W. R., Holden, H. M., Rayment, I. (1993) Structural consequences of reductive methylation of lysine residues in hen egg white lysozyme: An X-ray analysis at 1.8-A resolution. Biochemistry 32, 9851-9858.
    • (1993) Biochemistry , vol.32 , pp. 9851-9858
    • Rypniewski, W.R.1    Holden, H.M.2    Rayment, I.3


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