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Volumn 50, Issue 1, 2002, Pages 61-66

Thermal Glycation of Proteins by D-Glucose and D-Fructose

Author keywords

Bovine serum albumin; Conjugate; D fructose; D glucose; Glycation

Indexed keywords

ADVANCED GLYCATION END PRODUCT; BOVINE SERUM ALBUMIN; FRUCTOSE; GLUCOSE; PROTEIN;

EID: 1842863716     PISSN: 0004069X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (33)

References (28)
  • 1
    • 0030919275 scopus 로고    scopus 로고
    • N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methyiglyoxal, increases with age in human lens proteins
    • AHMED M. U., BRINKMANN-FRYE E., DEGENHARDT T. P., THORPE S. R. and BAYNES J. W. (1997): N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methyiglyoxal, increases with age in human lens proteins. Biochem. J., 324, 565-570.
    • (1997) Biochem. J. , vol.324 , pp. 565-570
    • Ahmed, M.U.1    Brinkmann-Frye, E.2    Degenhardt, T.P.3    Thorpe, S.R.4    Baynes, J.W.5
  • 2
    • 0022931516 scopus 로고
    • Identification of N-epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein
    • AHMED M. U., THORPE S. R. and BAYNES J. W. (1986): Identification of N-epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. J. Biol. Chem., 261, 4889-4894.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4889-4894
    • Ahmed, M.U.1    Thorpe, S.R.2    Baynes, J.W.3
  • 3
    • 84985269010 scopus 로고
    • Maillard browning of common amino acids and sugars
    • ASHOOR S. H. and ZENT J. B. (1984): Maillard browning of common amino acids and sugars. J. Food Sci., 49, 1206-1207.
    • (1984) J. Food Sci. , vol.49 , pp. 1206-1207
    • Ashoor, S.H.1    Zent, J.B.2
  • 4
    • 0025732948 scopus 로고
    • Role of oxidative stress in development of complications in diabetes
    • BAYNES J. W. (1991): Role of oxidative stress in development of complications in diabetes. Diabetes, 40, 405-412.
    • (1991) Diabetes , vol.40 , pp. 405-412
    • Baynes, J.W.1
  • 5
    • 0031715423 scopus 로고    scopus 로고
    • Dry reaction of proteins with carbohydrates at 120°C yields neoglycoconjugates
    • BORATYŃSKI J. (1998): Dry reaction of proteins with carbohydrates at 120°C yields neoglycoconjugates. Biotechnol. Techniques, 12, 707-710.
    • (1998) Biotechnol. Techniques , vol.12 , pp. 707-710
    • Boratyński, J.1
  • 6
    • 25544446846 scopus 로고    scopus 로고
    • BSE a consequence of introducing glucated host-unknown molecules to cattle?
    • in press
    • BORATYŃSKI J. and GÓRSKI A. (2002): BSE a consequence of introducing glucated host-unknown molecules to cattle? Med. Hypothesis (in press).
    • (2002) Med. Hypothesis
    • Boratyński, J.1    Górski, A.2
  • 7
    • 0031838928 scopus 로고    scopus 로고
    • High temperature conjugation of proteins with carbohydrates
    • BORATYŃSKI J. and ROY R. (1998): High temperature conjugation of proteins with carbohydrates. Glycoconjugate J., 15, 131-138.
    • (1998) Glycoconjugate J. , vol.15 , pp. 131-138
    • Boratyński, J.1    Roy, R.2
  • 8
    • 0027466334 scopus 로고
    • Transposition of an Alu-containing element induced by DNA-advanced glycosylation endproducts
    • BUCALA R., LEE A. T., ROURKE L. and CERAMI A. (1993): Transposition of an Alu-containing element induced by DNA-advanced glycosylation endproducts. Proc. Natl. Acad. Sci. USA, 90, 2666-2670.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2666-2670
    • Bucala, R.1    Lee, A.T.2    Rourke, L.3    Cerami, A.4
  • 9
    • 0034978333 scopus 로고    scopus 로고
    • How can thermal processing modify the antigenicity of proteins?
    • DAVIS P. J., SMALES C. M. and JAMES D. C. (2001): How can thermal processing modify the antigenicity of proteins? Allergy, 56, 56-60.
    • (2001) Allergy , vol.56 , pp. 56-60
    • Davis, P.J.1    Smales, C.M.2    James, D.C.3
  • 10
    • 0032500885 scopus 로고    scopus 로고
    • Sequencing of two alternatively spliced mRNAs corresponding to the extracellular domain of the rat receptor for advanced glycosylation end products (RAGE)
    • GIRÓN M. D., VARGAS A. M., SUAREZ M. D. and SALTO R. (1998): Sequencing of two alternatively spliced mRNAs corresponding to the extracellular domain of the rat receptor for advanced glycosylation end products (RAGE). Biochem. Biophys. Res. Commun., 251, 230-234.
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 230-234
    • Girón, M.D.1    Vargas, A.M.2    Suarez, M.D.3    Salto, R.4
  • 11
    • 0025948114 scopus 로고
    • Mechanism of formation of the Maillard protein cross-link pentosidine. Glucose, fructose, and ascorbate as pentosidine precursors
    • GRANHEE S. K. and MONNIER V. M. (1991): Mechanism of formation of the Maillard protein cross-link pentosidine. Glucose, fructose, and ascorbate as pentosidine precursors. J. Biol. Chem., 266, 11649-11653.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11649-11653
    • Granhee, S.K.1    Monnier, V.M.2
  • 12
    • 0024376977 scopus 로고
    • 3-Deoxyglucosone, an intermediate product of the Maillard reaction
    • KATO H., HAYASE F., SHIN D. B., OIMOMI M. and BABA S. (1989): 3-Deoxyglucosone, an intermediate product of the Maillard reaction. Prog. Clin. Biol. Res., 304, 69-84.
    • (1989) Prog. Clin. Biol. Res. , vol.304 , pp. 69-84
    • Kato, H.1    Hayase, F.2    Shin, D.B.3    Oimomi, M.4    Baba, S.5
  • 13
    • 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
  • 14
    • 0025540553 scopus 로고
    • Free radical generation by early glycation products: A mechanism for accelerated atherogenesis in diabetes
    • MULLARKEY C. J., EDELSTEIN D. and BROWNLEE M. (1990): Free radical generation by early glycation products: a mechanism for accelerated atherogenesis in diabetes. Biochem. Biophys. Res. Commun., 31, 932-939.
    • (1990) Biochem. Biophys. Res. Commun. , vol.31 , pp. 932-939
    • Mullarkey, C.J.1    Edelstein, D.2    Brownlee, M.3
  • 15
    • 0024308611 scopus 로고
    • The chemistry of the Maillard reaction under physiological conditions: A review
    • NJOROGE F. G. and MONNIER V. M. (1989): The chemistry of the Maillard reaction under physiological conditions: a review. Prog. Clin. Biol. Res., 304, 85-107.
    • (1989) Prog. Clin. Biol. Res. , vol.304 , pp. 85-107
    • Njoroge, F.G.1    Monnier, V.M.2
  • 16
    • 0013820366 scopus 로고
    • Chemistry of nonenzymic browning. II
    • REYNOLDS T. M. (1965): Chemistry of nonenzymic browning. II. Adv. Food Res., 14, 167-283.
    • (1965) Adv. Food Res. , vol.14 , pp. 167-283
    • Reynolds, T.M.1
  • 17
    • 0027176945 scopus 로고
    • Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products
    • SCHMIDT A. M., YAN S. D., BRETT J., MORA R., NOWYGROD R. and STERN D. (1993): Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products. J. Clin. Invest., 91, 2155-2168.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2155-2168
    • Schmidt, A.M.1    Yan, S.D.2    Brett, J.3    Mora, R.4    Nowygrod, R.5    Stern, D.6
  • 18
    • 0024852380 scopus 로고
    • Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process
    • SELL D. R. and MONNIER V. M. (1989): Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process. J. Biol. Chem., 264, 21597-21602.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21597-21602
    • Sell, D.R.1    Monnier, V.M.2
  • 19
    • 0028053731 scopus 로고
    • Monitoring the progress of non-enzymatic glycation in vitro
    • SHAW S. M. and CRABBE M. J. C. (1994): Monitoring the progress of non-enzymatic glycation in vitro. Int. J. Pept. Protein Res., 44, 594-602.
    • (1994) Int. J. Pept. Protein Res. , vol.44 , pp. 594-602
    • Shaw, S.M.1    Crabbe, M.J.C.2
  • 20
    • 0025874366 scopus 로고
    • Fructose-induced fluorescence generation of reductively methylated glycated bovine serum albumin: Evidence for nonenzymatic glycation of Amadori adducts
    • SUÁREZ G., MUTARANA J., ORONSKY A. L. and RAVENTÓS-SUAREZ C. (1991): Fructose-induced fluorescence generation of reductively methylated glycated bovine serum albumin: Evidence for nonenzymatic glycation of Amadori adducts. Biochim. Biophys. Acta, 1075, 12-19.
    • (1991) Biochim. Biophys. Acta , vol.1075 , pp. 12-19
    • Suárez, G.1    Mutarana, J.2    Oronsky, A.L.3    Raventós-Suarez, C.4
  • 21
    • 0033571012 scopus 로고    scopus 로고
    • Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
    • THORNALLEY P. J., LANGBORG A. and MINHAS H. S. (1999): Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem. J., 344, 109-116.
    • (1999) Biochem. J. , vol.344 , pp. 109-116
    • Thornalley, P.J.1    Langborg, A.2    Minhas, H.S.3
  • 22
    • 0029763759 scopus 로고    scopus 로고
    • Role of the Maillard reaction in diabetes mellitus and diseases of aging
    • THORPE S. R. and BAYNES J. W. (1996): Role of the 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
  • 24
    • 0034670095 scopus 로고    scopus 로고
    • Inhibition of nitric oxide synthase activity by early and advanced glycation end products in cultured rabbit proximal tubular epithelial cells
    • VERBEKE P., PERICHON M., FRIGUET B. and BAKALA H. (2000): Inhibition of nitric oxide synthase activity by early and advanced glycation end products in cultured rabbit proximal tubular epithelial cells. Biochim. Biophys. Acta, 15, 481-494.
    • (2000) Biochim. Biophys. Acta , vol.15 , pp. 481-494
    • Verbeke, P.1    Perichon, M.2    Friguet, B.3    Bakala, H.4
  • 25
    • 0023940640 scopus 로고
    • Cachectin/TNF and IL-1 induced by glucose-modified proteins: Role in normal tissue remodeling
    • VLASSARA H., BROWNLEE M., MANOGUE K. R., DINARELLO C. A. and PASAGIAN A. (1988): Cachectin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling. Science, 240, 1546-1548.
    • (1988) Science , vol.240 , pp. 1546-1548
    • Vlassara, H.1    Brownlee, M.2    Manogue, K.R.3    Dinarello, C.A.4    Pasagian, A.5
  • 27
    • 0028233384 scopus 로고
    • The endothelial cell binding site for advanced glycation end products consists of a complex: An integral membrane protein and a lactoferrin-like polypeptide
    • YAN S. D., SCHMIDT A. M., ANDERSON G. M., ZHANG J., BRETT J., ZOU Y. S., PINSKY D. and STERN D. (1994): The endothelial cell binding site for advanced glycation end products consists of a complex: an integral membrane protein and a lactoferrin-like polypeptide. J. Biol. Chem., 269, 9889-9897.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9889-9897
    • Yan, S.D.1    Schmidt, A.M.2    Anderson, G.M.3    Zhang, J.4    Brett, J.5    Zou, Y.S.6    Pinsky, D.7    Stern, D.8
  • 28
    • 0032864734 scopus 로고    scopus 로고
    • Reactivities of D-glucose and D-fructose during glycation of bovine serum albumin
    • YEBOAH F. K., ALLI I. and YAYLAYAN V. A. (1999): Reactivities of D-glucose and D-fructose during glycation of bovine serum albumin. J. Agric. Food Chem., 47, 3164-3172.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 3164-3172
    • Yeboah, F.K.1    Alli, I.2    Yaylayan, V.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.