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Volumn 30, Issue 1, 2011, Pages 5-10

A biophysical comparison of human serum albumin to be glycated in vivo and in vitro

Author keywords

arginine residue; diabetic individual; glycation; human serum albumin

Indexed keywords

1,2 DICARBONYL DERIVATIVE; 3 DEOXYGLUCOSONE; ADVANCED GLYCATION END PRODUCT; ARGININE; HUMAN SERUM ALBUMIN; SCHIFF BASE;

EID: 78649668281     PISSN: 14528258     EISSN: 14528266     Source Type: Journal    
DOI: 10.2478/v10011-010-0026-7     Document Type: Article
Times cited : (13)

References (27)
  • 1
    • 0033551042 scopus 로고    scopus 로고
    • Ama do rins: novel post-Amadori inhibitors of advanced glycation reac tions
    • Khalifah RG, Baynes JW, Hudson BG. Ama do rins: novel post-Amadori inhibitors of advanced glycation reac tions. Biochem Biophys Res Commun 1999; 257: 251-8.
    • (1999) Biochem Biophys Res Commun , vol.257 , pp. 251-8
    • Khalifah, R.G.1    Baynes, J.W.2    Hudson, B.G.3
  • 2
    • 11844292005 scopus 로고    scopus 로고
    • Importance of measuring products of non-enzymatic glycation of proteins
    • Lapolla A, Traldi P, Fedele D. Importance of measuring products of non-enzymatic glycation of proteins. Clin Biochem 2005; 38: 103-15.
    • (2005) Clin Biochem , vol.38 , pp. 103-15
    • Lapolla, A.1    Traldi, P.2    Fedele, D.3
  • 3
    • 0021365056 scopus 로고
    • Nonenzymatic glycosylation of human serum albumin alters its confor mation and function
    • Shaklai N, Garlick RL, Bunn H F. Nonenzymatic glycosylation of human serum albumin alters its confor mation and function. J Biol Chem 1984; 259 (6): 3812-7.
    • (1984) J Biol Chem , vol.259 , Issue.6 , pp. 3812-7
    • Shaklai, N.1    Garlick, R.L.2    Bunn, H.F.3
  • 5
    • 0141671890 scopus 로고    scopus 로고
    • Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation
    • Cussimanio BL, Booth AA, Todd P, Hudson BG, Khalifah RG. Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation. Biophys Chem 2003; 105: 43-755.
    • (2003) Biophys Chem , vol.105 , pp. 43-755
    • Cussimanio, B.L.1    Booth, A.A.2    Todd, P.3    Hudson, B.G.4    Khalifah, R.G.5
  • 7
    • 0026664548 scopus 로고
    • Atomic structure and che mi stry of human serum albumin
    • He XM, Carter DC. Atomic structure and che mi stry of human serum albumin. Nature 1992; 358: 209-15.
    • (1992) Nature , vol.358 , pp. 209-15
    • He, X.M.1    Carter, D.C.2
  • 9
    • 0032966525 scopus 로고    scopus 로고
    • Glucose and free radicals impair the antioxidant properties of serum albumin
    • Bourdon E, Loreau N, Blache D. Glucose and free radicals impair the antioxidant properties of serum albumin. FASEB J 1999; 13: 233-43.
    • (1999) FASEB J , vol.13 , pp. 233-43
    • Bourdon, E.1    Loreau, N.2    Blache, D.3
  • 10
    • 0023009324 scopus 로고
    • Nonenzymatic glyco sylation of albumin in vitro (Identification of multiple glycosylated sites)
    • Iberg N, Fluckiger R. Nonenzymatic glyco sylation of albumin in vitro (Identification of multiple glycosylated sites). J Biol Chem 1986; 261: 13542-5.
    • (1986) J Biol Chem , vol.261 , pp. 13542-5
    • Iberg, N.1    Fluckiger, R.2
  • 12
    • 0036699372 scopus 로고    scopus 로고
    • Ama-dori product and AGE formation during nonenzymatic glycosylation of bovine serum albumin In Vitro
    • Sharma SD, Pandey BN, Mishra K P, Sivakami S. Amadori product and AGE formation during nonenzymatic glycosylation of bovine serum albumin In Vitro. J Biochem Mol Biol Biophys 2002; 6 (4): 233-42.
    • (2002) J Biochem Mol Biol Biophys , vol.6 , Issue.4 , pp. 233-42
    • Sharma, S.D.1    Pandey, B.N.2    Mishra, K.P.3    Sivakami, S.4
  • 13
    • 0021365056 scopus 로고
    • Nonenzymatic gly cosylation of human serum albumin alters its conformation and function
    • Shaklai N, Garlick RL, Bunn H F. Nonenzymatic gly cosylation of human serum albumin alters its conformation and function. J Biol Chem 1984; 259 (6): 3812-7.
    • (1984) J Biol Chem , vol.259 , Issue.6 , pp. 3812-7
    • Shaklai, N.1    Garlick, R.L.2    Bunn, H.F.3
  • 17
    • 0029165873 scopus 로고
    • Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation end product-modi fied serum albumins
    • Westwood ME, Thornalley PJ. Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation end product-modi fied serum albumins. J Protein Chem 1995; 4: 359-72.
    • (1995) J Protein Chem , vol.4 , pp. 359-72
    • Westwood, M.E.1    Thornalley, P.J.2
  • 18
    • 0037067723 scopus 로고    scopus 로고
    • Identi fi cation and quantification of major Maillard cross-links in human serum albumin and lens protein
    • Biemel KM, Friedl DA, Lederer MO. Identi fi cation and quantification of major Maillard cross-links in human serum albumin and lens protein. J Biol Chem 2002; 277: 24907-15.
    • (2002) J Biol Chem , vol.277 , pp. 24907-15
    • Biemel, K.M.1    Friedl, D.A.2    Lederer, M.O.3
  • 22
    • 33646866573 scopus 로고    scopus 로고
    • Affinity adsorption of albumin on Cibacron Blue F3GA-coupled non-porous micrometer-sized magnetic polymer microspheres
    • Ma Z Y, Guan Y P, Liu HZ. Affinity adsorption of albumin on Cibacron Blue F3GA-coupled non-porous micrometer-sized magnetic polymer microspheres. React Funct Polym 2006; 66: 618-24.
    • (2006) React Funct Polym , vol.66 , pp. 618-24
    • Ma, Z.Y.1    Guan, Y.P.2    Liu, H.Z.3
  • 23
    • 0020174776 scopus 로고
    • Charac te rization of fragments of human albumin purified by Cibacron Blue F3GA affinity chromatography
    • Ledden DJ, Feldhoff RC, Chan SK. Charac te rization of fragments of human albumin purified by Cibacron Blue F3GA affinity chromatography. Biochem J 1982; 205: 331-7.
    • (1982) Biochem J , vol.205 , pp. 331-7
    • Ledden, D.J.1    Feldhoff, R.C.2    Chan, S.K.3
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5.
    • (1970) Nature , vol.227 , pp. 680-5
    • Laemmli, U.K.1
  • 25
    • 0020687017 scopus 로고
    • Staining of proteins on gels: Compa rison of dyes and procedures
    • Wilson C. Staining of proteins on gels: compa rison of dyes and procedures. Methods Enzymol 1983; 91: 236-47.
    • (1983) Methods Enzymol , vol.91 , pp. 236-47
    • Wilson, C.1
  • 26
    • 14644397841 scopus 로고    scopus 로고
    • Characterization of advanced glycation end products for bioche mical studies: Side chain modifications and fluorescence characteristics
    • Schmitt A, Schmitt J, Münch G, Gasic-Milencovic J. Characterization of advanced glycation end products for bioche mical studies: side chain modifications and fluorescence characteristics. Anal Biochem 2005; 338: 201-15.
    • (2005) Anal Biochem , vol.338 , pp. 201-15
    • Schmitt, A.1    Schmitt, J.2    Münch, G.3    Gasic-Milencovic, J.4
  • 27
    • 77955248678 scopus 로고    scopus 로고
    • Genetic predisposition for type 1 diabetes mellitus the Role of endoplasmic reticulum stress in human disease etiopathogenesis
    • Stankov K. Genetic predisposition for type 1 diabetes mellitus The Role of endoplasmic reticulum stress in human disease etiopathogenesis. Journal od Medical Biochemistry 2010; 29: 139-49.
    • (2010) Journal Od Medical Biochemistry , vol.29 , pp. 139-49
    • Stankov, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.