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Volumn 47, Issue 8, 1999, Pages 3164-3172

Reactivities of D-glucose and D-fructose during glycation of bovine serum albumin

Author keywords

BSA; Cross linking; D fructose; D glucose; Fluorescence; Glycation; Reactivitiy

Indexed keywords

BOVINE SERUM ALBUMIN; FRUCTOSE; GLUCOSE; GLYCOSYLATED SERUM ALBUMIN; SERUM ALBUMIN;

EID: 0032864734     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf981289v     Document Type: Article
Times cited : (111)

References (39)
  • 1
    • 84986517519 scopus 로고
    • Free amino acid stability in reducing sugar systems
    • Baxter, H. J. Free amino acid stability in reducing sugar systems. J. Food Sci. 1995, 60 (2), 405-408
    • (1995) J. Food Sci. , vol.60 , Issue.2 , pp. 405-408
    • Baxter, H.J.1
  • 3
    • 0027956982 scopus 로고
    • Modification of low-density lipoprotein by advanced glycation end products contribute to the dyslipidemia of diabetes and renal insufficiency
    • Bucala, R.; Makita, Z.; Vega, G.; Grundy, S.; Koschinsky, T.; Cerami, A.; Vlassara, H. Modification of low-density lipoprotein by advanced glycation end products contribute to the dyslipidemia of diabetes and renal insufficiency. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 9441-9445.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 9441-9445
    • Bucala, R.1    Makita, Z.2    Vega, G.3    Grundy, S.4    Koschinsky, T.5    Cerami, A.6    Vlassara, H.7
  • 4
    • 0019796775 scopus 로고
    • Reactions of monosaccharides with proteins: Possible evolutionary significance
    • Bunn, H. F.; Higgins, P. J. Reactions of monosaccharides with proteins: possible evolutionary significance. Science 1981, 213, 222-224.
    • (1981) Science , vol.213 , pp. 222-224
    • Bunn, H.F.1    Higgins, P.J.2
  • 6
    • 0027445113 scopus 로고
    • Protein fructosylation: Fructose and the Maillard reaction
    • Dills, L. W. Protein fructosylation: Fructose and the Maillard reaction. Am. J. Clin. Nutr. 1993, 58 (Suppl.), 779S-787S.
    • (1993) Am. J. Clin. Nutr. , vol.58 , Issue.SUPPL.
    • Dills, L.W.1
  • 7
    • 0017437920 scopus 로고
    • Humidity fixed points of binary saturated aqueous solutions
    • Greenespan, L. Humidity fixed points of binary saturated aqueous solutions. J. Res. Natl. Bur. Stand. 1977, 81A, 89-96.
    • (1977) J. Res. Natl. Bur. Stand. , vol.81 A , pp. 89-96
    • Greenespan, L.1
  • 8
    • 0002759996 scopus 로고
    • Influence of the Maillard reaction on the nutritional value of foods
    • Finot, P. A., Aeschbacher, H. U., Hurrel, R. F., Liardon, R., Eds.; Birkhauser Verlag: Basel, Switzerland
    • Hurrel, R. F. Influence of the Maillard reaction on the nutritional value of foods. In The Maillard Reaction in Food Processing, Human Nutrtition and Physiology; Finot, P. A., Aeschbacher, H. U., Hurrel, R. F., Liardon, R., Eds.; Birkhauser Verlag: Basel, Switzerland, 1990; pp 245-258.
    • (1990) The Maillard Reaction in Food Processing, Human Nutrtition and Physiology , pp. 245-258
    • Hurrel, R.F.1
  • 9
    • 0024986845 scopus 로고
    • Functional protein-polysaccharide conjugate prepared by controlled dry-heating of ovalbumin dextran mixtures
    • Kato, A.; Sasaki, Y.; Furuta, R.; Kobayashi, K. Functional protein-polysaccharide conjugate prepared by controlled dry-heating of ovalbumin dextran mixtures. J. Agric. Biol. Chem. 1990, 54, 107-112.
    • (1990) J. Agric. Biol. Chem. , vol.54 , pp. 107-112
    • Kato, A.1    Sasaki, Y.2    Furuta, R.3    Kobayashi, K.4
  • 10
    • 0001212535 scopus 로고
    • Improvement of the functional prpperties of insoluble gluten by Pronase digestion followed by dextran conjugation
    • Kato, A.; Shimokawa, K.; Kobayashi, K. Improvement of the functional prpperties of insoluble gluten by Pronase digestion followed by dextran conjugation. J. Agric. Food Chem. 1991, 39 (6), 1053-1056.
    • (1991) J. Agric. Food Chem. , vol.39 , Issue.6 , pp. 1053-1056
    • Kato, A.1    Shimokawa, K.2    Kobayashi, K.3
  • 11
    • 0343703751 scopus 로고    scopus 로고
    • Novel functional properties of glycosylated lysozyme constructed by chemical and genetic modifications
    • ACS Symposium Series 650; American Chemical Society: Washington, DC
    • Kato, A.; Nakamura, S.; Takasaki, H.; Maki, S. Novel functional properties of glycosylated lysozyme constructed by chemical and genetic modifications. In Macromolecular Interactions in Food Technology; ACS Symposium Series 650; American Chemical Society: Washington, DC, 1996; pp 243-256.
    • (1996) Macromolecular Interactions in Food Technology , pp. 243-256
    • Kato, A.1    Nakamura, S.2    Takasaki, H.3    Maki, S.4
  • 12
    • 0001703298 scopus 로고
    • Mechanisms of browning degradation of D-fructose in spercial comparison with D-glucose-glycine reaction
    • Kato, H.; Yamamoto, M.; Fujimaki, M. Mechanisms of browning degradation of D-fructose in spercial comparison with D-glucose-glycine reaction. J. Agric. Food Chem. 1969, 33, 939-948.
    • (1969) J. Agric. Food Chem. , vol.33 , pp. 939-948
    • Kato, H.1    Yamamoto, M.2    Fujimaki, M.3
  • 14
    • 0002283646 scopus 로고
    • The kinetics of nonenzymatic browning
    • Schwartzberg, H. G., Hastel, R. W., Eds.; IFT Basic Symposium Series 7; Dekker: New York
    • Labuza, T. P.; Baisier, W. M. The kinetics of nonenzymatic browning. In Physical Chemistry of Foods; Schwartzberg, H. G., Hastel, R. W., Eds.; IFT Basic Symposium Series 7; Dekker: New York, 1992; pp 595-689.
    • (1992) Physical Chemistry of Foods , pp. 595-689
    • Labuza, T.P.1    Baisier, W.M.2
  • 15
    • 84985204539 scopus 로고
    • Kinetics of browning and protein quality loss in whey powders during steady state and non-steady-state storage conditions
    • Labuza, T. P.; Saltmarch, M. Kinetics of browning and protein quality loss in whey powders during steady state and non-steady-state storage conditions. J. Food Sci. 1981, 47, 92-96, 113.
    • (1981) J. Food Sci. , vol.47 , pp. 92-96
    • Labuza, T.P.1    Saltmarch, M.2
  • 17
    • 21344456480 scopus 로고    scopus 로고
    • Bovin serum albumin gelation as a result of the Maillard reaction
    • Mat Easa, A.; Hill, S. E.; Mitchell, J. R.; Taylor, A. J. Bovin serum albumin gelation as a result of the Maillard reaction. Food Hydrocolloids 1996, 10, 199-202.
    • (1996) Food Hydrocolloids , vol.10 , pp. 199-202
    • Mat Easa, A.1    Hill, S.E.2    Mitchell, J.R.3    Taylor, A.J.4
  • 18
    • 0019762671 scopus 로고
    • The Maillard reaction in food: A critical review from the nutritional standpoint
    • Mauron, J. The Maillard reaction in food: A critical review from the nutritional standpoint. Prog. Food Sci. 1981, 5, 5-35.
    • (1981) Prog. Food Sci. , vol.5 , pp. 5-35
    • Mauron, J.1
  • 19
    • 0001430544 scopus 로고
    • Accelerated age-related browning of human collagen in diabetes mellitus
    • Monnier, V. M.; Kohn, R. R.; Cerami, A. Accelerated age-related browning of human collagen in diabetes mellitus. Proc. Natl Acad. Sci. USA. 1984, 81, 583-587.
    • (1984) Proc. Natl Acad. Sci. USA. , vol.81 , pp. 583-587
    • Monnier, V.M.1    Kohn, R.R.2    Cerami, A.3
  • 20
    • 0030297917 scopus 로고    scopus 로고
    • Fluorescence associated with Maillard reaction in milk-resembling systems
    • Morales, J. F.; Romero, C.; Jimenez-Perez, S. Fluorescence associated with Maillard reaction in milk-resembling systems. Food Chem. 1996, 57 (3), 423-428.
    • (1996) Food Chem. , vol.57 , Issue.3 , pp. 423-428
    • Morales, J.F.1    Romero, C.2    Jimenez-Perez, S.3
  • 21
    • 0000774327 scopus 로고    scopus 로고
    • Degradation of tryptophane in heated β-lactoglobulin-lactose mixtures is associated with intense Maillard reaction
    • Moreaux, V.; Birlouez-Aragon, I. Degradation of tryptophane in heated β-lactoglobulin-lactose mixtures is associated with intense Maillard reaction. J. Agric. Food Chem. 1997, 45, 1905-1910.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1905-1910
    • Moreaux, V.1    Birlouez-Aragon, I.2
  • 22
    • 33751500314 scopus 로고
    • New antimicrobial characteristics of lysozyme-dextranconjugate
    • Nakamura, S.; Kato, A.; Kobayashi, K. New antimicrobial characteristics of lysozyme-dextranconjugate. J. Agric. Food Chem. 1991, 39, 645-650.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 645-650
    • Nakamura, S.1    Kato, A.2    Kobayashi, K.3
  • 23
    • 0000668338 scopus 로고
    • Enhanced antioxidative effect of ovalbumin due to covalent binding of polysacchrides
    • Nakamura, S.; Kato, A.; Kobayashi, K. Enhanced antioxidative effect of ovalbumin due to covalent binding of polysacchrides. J. Agric. Food Chem. 1992a, 40, 2033-2037.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 2033-2037
    • Nakamura, S.1    Kato, A.2    Kobayashi, K.3
  • 24
    • 33751391825 scopus 로고
    • Bifunctional lysozyme-galactomannan conjugate having excellent emulcifying properties and antibacterial effects
    • Nakamura, S.; Kato, A.; Kobayashi, K. Bifunctional lysozyme-galactomannan conjugate having excellent emulcifying properties and antibacterial effects. J. Agric. Food Chem. 1992b, 40, 735-739.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 735-739
    • Nakamura, S.1    Kato, A.2    Kobayashi, K.3
  • 25
    • 0032127597 scopus 로고    scopus 로고
    • Reducing sugar effect on available lysine loss of casein by moderate heat treatment
    • Naranjo, G. B.; Malec, L. S.; Vigo, M. S. Reducing sugar effect on available lysine loss of casein by moderate heat treatment. Food Chem. 1998, 62, 309-313.
    • (1998) Food Chem. , vol.62 , pp. 309-313
    • Naranjo, G.B.1    Malec, L.S.2    Vigo, M.S.3
  • 26
    • 0032492551 scopus 로고    scopus 로고
    • The generation of superoxide anions in glycation reactions with sugars, osones and 3-deoxyosones
    • Ortwerth, B. J.; James, H.; Simpson, G.; Linetsky, M. The generation of superoxide anions in glycation reactions with sugars, osones and 3-deoxyosones. Biochem. Biophys. Res. Commun. 1998, 245 (1), 161-165.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , Issue.1 , pp. 161-165
    • Ortwerth, B.J.1    James, H.2    Simpson, G.3    Linetsky, M.4
  • 28
    • 84982382809 scopus 로고
    • Role of amino acids in nonenzymic bowning
    • Spark, A. A. Role of amino acids in nonenzymic bowning. J. Sci. Food Agric. 1969, 20, 308-316.
    • (1969) J. Sci. Food Agric. , vol.20 , pp. 308-316
    • Spark, A.A.1
  • 29
    • 0024514306 scopus 로고
    • Nonenzymatic glycation of bovin serum albumin by fructose (Fructation), comparison with the Maillard reaction initiated by glucose
    • Suarez, G.; Rajaram, R.; Oronsky, A. L.; Gawinowicz, M. A. Nonenzymatic glycation of bovin serum albumin by fructose (Fructation), comparison with the Maillard reaction initiated by glucose. J. Biol. Chem. 1989, 264, 3674-3679.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3674-3679
    • Suarez, G.1    Rajaram, R.2    Oronsky, A.L.3    Gawinowicz, M.A.4
  • 30
    • 0025874366 scopus 로고
    • Fructose induced fluorescence generation of reductively methylated glycated bovin serum albumin: Evidence for nonemzymatic glycation of Amadori products
    • Suarez, G.; Maturana, J.; Oronsky, A. L.; Raventos-Suarez, C. Fructose induced fluorescence generation of reductively methylated glycated bovin serum albumin: evidence for nonemzymatic glycation of Amadori products. Biochim. Biophys Acta 1991, 1075, 12-19.
    • (1991) Biochim. Biophys Acta , vol.1075 , pp. 12-19
    • Suarez, G.1    Maturana, J.2    Oronsky, A.L.3    Raventos-Suarez, C.4
  • 31
    • 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
    • Suarez, G.; Etlinger, D. J.; Maturana, J.; Weitman, D. 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. 1995, 321 (1), 209-213.
    • (1995) Arch. Biochem. Biophys. , vol.321 , Issue.1 , pp. 209-213
    • Suarez, G.1    Etlinger, D.J.2    Maturana, J.3    Weitman, D.4
  • 32
    • 0021361665 scopus 로고
    • The autoxidation of glyceraldehyde and other simple monosaccherides under physiological conditions catalysed by buffer ions
    • Thornalley, P.; Wolff, S.; Crabbe, J.; Stern A. The autoxidation of glyceraldehyde and other simple monosaccherides under physiological conditions catalysed by buffer ions. Biochim. Biophys. Acta 1984, 797, 276-287.
    • (1984) Biochim. Biophys. Acta , vol.797 , pp. 276-287
    • Thornalley, P.1    Wolff, S.2    Crabbe, J.3    Stern, A.4
  • 33
    • 0031801458 scopus 로고    scopus 로고
    • Digestibility and peptide patterns of modified lysozyme after hydrolyzing by protease
    • Umetsu, H.; Van Chuyen, N. Digestibility and peptide patterns of modified lysozyme after hydrolyzing by protease. J. Nutr. Sci. Vitaminol. 1998, 44, 291-300.
    • (1998) J. Nutr. Sci. Vitaminol. , vol.44 , pp. 291-300
    • Umetsu, H.1    Van Chuyen, N.2
  • 35
    • 0010233525 scopus 로고
    • Glucose-lysozyme in a restricted water environment
    • Finot, P. A., Aeschbacher, H. U., Hurrel, R. F., Liardon, R., Eds.; Birkhauser Verlag: Basel, Switzerland
    • Wu, H.; Govidarajan, S.; Smith, T.; Rosen, J. D.; Ho, C.-T. Glucose-lysozyme in a restricted water environment. In The Maillard Reaction in Food Processing, Human Nutrtition and Physiology; Finot, P. A., Aeschbacher, H. U., Hurrel, R. F., Liardon, R., Eds.; Birkhauser Verlag: Basel, Switzerland, 1990; pp 85-90.
    • (1990) The Maillard Reaction in Food Processing, Human Nutrtition and Physiology , pp. 85-90
    • Wu, H.1    Govidarajan, S.2    Smith, T.3    Rosen, J.D.4    Ho, C.-T.5
  • 36
    • 0031040322 scopus 로고    scopus 로고
    • Classification of the Maillard reaction: A conceptual approach
    • Yaylayan, A. V. Classification of the Maillard reaction: A conceptual approach. Trends Food Sci. Technol. 1997, 8, 13-18.
    • (1997) Trends Food Sci. Technol. , vol.8 , pp. 13-18
    • Yaylayan, A.V.1
  • 37
    • 0028247972 scopus 로고
    • Chemistry of Amadori rearrangement products: Analysis, synthesis, kinetics, reactions and spectroscopic properties
    • Yaylayan, A. V.; Huyghues-Despointes, A. Chemistry of Amadori rearrangement products: analysis, synthesis, kinetics, reactions and spectroscopic properties. Crit. Rev. Food Sci. Nutr. 1994, 34 (4), 321-369.
    • (1994) Crit. Rev. Food Sci. Nutr. , vol.34 , Issue.4 , pp. 321-369
    • Yaylayan, A.V.1    Huyghues-Despointes, A.2
  • 38
    • 44949266848 scopus 로고
    • A fluorescamine-based assay for the degree of glycation in bovine serum albumin
    • Yaylayan, A. V.; Huyghues-Despointes, A.; Polydorides, A. A fluorescamine-based assay for the degree of glycation in bovine serum albumin. Food Res. Int. 1992, 25, 269-275.
    • (1992) Food Res. Int. , vol.25 , pp. 269-275
    • Yaylayan, A.V.1    Huyghues-Despointes, A.2    Polydorides, A.3
  • 39
    • 0027908695 scopus 로고
    • Quantitative determination of the effect of pH and temperature on the keto form of D-fructose by FTIR spectroscopy
    • Yaylayan, A. V.; Ismail, A. A.; Mandeville, S. Quantitative determination of the effect of pH and temperature on the keto form of D-fructose by FTIR spectroscopy. Carbohydr. Res. 1993, 248, 355-360.
    • (1993) Carbohydr. Res. , vol.248 , pp. 355-360
    • Yaylayan, A.V.1    Ismail, A.A.2    Mandeville, S.3


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