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Volumn 20, Issue 4, 2003, Pages 684-692

Validation of the chloramine-T induced oxidation of human serum albumin as a model for oxidative damage in vivo

Author keywords

Chloramine T; Cysteine mutation; Human serum albumin; Oxidative damage; Pharmacokinetics; Site II

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); CYANOGEN BROMIDE; CYSTEINE; HUMAN SERUM ALBUMIN; KETOPROFEN; METHIONINE; TOSYLCHLORAMIDE SODIUM; TRYPTOPHAN; WARFARIN;

EID: 12444344290     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1023219420935     Document Type: Article
Times cited : (46)

References (26)
  • 1
    • 0024443449 scopus 로고
    • Derivatization of γ-glutamyl semialdehyde residues in oxidized proteins by fluoresceinamine
    • I. Climent, L. Tsai, and R. L. Levine. Derivatization of γ-glutamyl semialdehyde residues in oxidized proteins by fluoresceinamine. Anal. Biochem. 182:226-232 (1989).
    • (1989) Anal. Biochem. , vol.182 , pp. 226-232
    • Climent, I.1    Tsai, L.2    Levine, R.L.3
  • 2
    • 0032966525 scopus 로고    scopus 로고
    • Glucose and free radicals impair the antioxidant properties of serum albumin
    • E. Bourdon, N. Loreau, and D. Blache. Glucose and free radicals impair the antioxidant properties of serum albumin. FASEB J. 13:233-244 (1999).
    • (1999) FASEB J. , vol.13 , pp. 233-244
    • Bourdon, E.1    Loreau, N.2    Blache, D.3
  • 3
  • 4
    • 0034959203 scopus 로고    scopus 로고
    • Effect of oxidative stress on the structure and function of human serum albumin
    • M. Anraku, K. Yamasaki, T. Maruyama, U. Kragh-Hansen, and M. Otagiri. Effect of oxidative stress on the structure and function of human serum albumin. Pharm. Res. 18:632-639 (2001).
    • (2001) Pharm. Res. , vol.18 , pp. 632-639
    • Anraku, M.1    Yamasaki, K.2    Maruyama, T.3    Kragh-Hansen, U.4    Otagiri, M.5
  • 5
    • 0023881390 scopus 로고
    • Further studies on the resolution of human mercapt- and non-mercaptalbumin and on human serum albumin in the elderly by high-performance liquid chromatography
    • S. Era, T. Hamaguchi, M. Sogami, K. Kuwata, E. Suzuki, K. Miura, K. Kawai, Y. Kitazawa, H. Okabe, A. Noma, and S. Miyata. Further studies on the resolution of human mercapt- and non-mercaptalbumin and on human serum albumin in the elderly by high-performance liquid chromatography. Int. J. Pept. Protein Res. 31:435-442 (1988).
    • (1988) Int. J. Pept. Protein Res. , vol.31 , pp. 435-442
    • Era, S.1    Hamaguchi, T.2    Sogami, M.3    Kuwata, K.4    Suzuki, E.5    Miura, K.6    Kawai, K.7    Kitazawa, Y.8    Okabe, H.9    Noma, A.10    Miyata, S.11
  • 6
    • 0021154659 scopus 로고
    • Resolution of human mercapt and nonmercaptalbumin by high performance liquid chromatography
    • M. Sogami, S. Nagaoka, S. Era, M. Honda, and K. Noguchi. Resolution of human mercapt and nonmercaptalbumin by high performance liquid chromatography. Int. J. Pept. Protein Res. 24:96-103 (1984).
    • (1984) Int. J. Pept. Protein Res. , vol.24 , pp. 96-103
    • Sogami, M.1    Nagaoka, S.2    Era, S.3    Honda, M.4    Noguchi, K.5
  • 8
    • 0016786370 scopus 로고
    • Selective oxidation of methionine residues in proteins
    • Y. Shechter, Y. Burstein, and A. Patchornik. Selective oxidation of methionine residues in proteins. Biochemistry 14:4497-4503 (1975).
    • (1975) Biochemistry , vol.14 , pp. 4497-4503
    • Shechter, Y.1    Burstein, Y.2    Patchornik, A.3
  • 9
    • 0014216041 scopus 로고
    • Removal of fatty acids from serum albumin by charcoal treatment
    • R. F. Chen. Removal of fatty acids from serum albumin by charcoal treatment. J. Biol. Chem. 242:173-181 (1967).
    • (1967) J. Biol. Chem. , vol.242 , pp. 173-181
    • Chen, R.F.1
  • 11
    • 0035659618 scopus 로고    scopus 로고
    • In vitro and in vivo properties of recombinant human serum albumin from Pichia pastoris purified by a method of short processing time
    • H. Watanabe, K. Yamasaki, U. Kragh-Hansen, S. Tanase, K. Harada, A. Suenaga, and M. Otagiri. In vitro and in vivo properties of recombinant human serum albumin from Pichia pastoris purified by a method of short processing time. Pharm. Res. 18:1775-1781 (2001).
    • (2001) Pharm. Res. , vol.18 , pp. 1775-1781
    • Watanabe, H.1    Yamasaki, K.2    Kragh-Hansen, U.3    Tanase, S.4    Harada, K.5    Suenaga, A.6    Otagiri, M.7
  • 12
    • 0033958443 scopus 로고    scopus 로고
    • Observation for redox state of human serum and aqueous humor albumin from patients with senile cataract
    • T. Hayashi, S. Era, K. Kawai, H. Imai, K. Nakamura, E. Onda, and M. Yoh. Observation for redox state of human serum and aqueous humor albumin from patients with senile cataract. Pathophysiology 6:237-243 (2000).
    • (2000) Pathophysiology , vol.6 , pp. 237-243
    • Hayashi, T.1    Era, S.2    Kawai, K.3    Imai, H.4    Nakamura, K.5    Onda, E.6    Yoh, M.7
  • 13
    • 0021039330 scopus 로고
    • Coupling between fatty acid binding and sulfhydryl oxidation in bovine serum albumin
    • K. Takabayashi, T. Imada, Y. Saito, and Y. Inada. Coupling between fatty acid binding and sulfhydryl oxidation in bovine serum albumin. Eur. J. Biochem. 136:291-295 (1983).
    • (1983) Eur. J. Biochem. , vol.136 , pp. 291-295
    • Takabayashi, K.1    Imada, T.2    Saito, Y.3    Inada, Y.4
  • 14
    • 0029917011 scopus 로고    scopus 로고
    • Linearization of the Bradford protein assay increases its sensitivity: Theoretical and experimental studies
    • T. Zor and Z. Selinger. Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies. Anal. Biochem. 236:302-308 (1996).
    • (1996) Anal. Biochem. , vol.236 , pp. 302-308
    • Zor, T.1    Selinger, Z.2
  • 15
    • 0026723384 scopus 로고
    • Optimization and validation of analytical conditions for bovine serum albumin using capillary electrophoresis
    • P. G. Pande, R. V. Nellore, and H. R. Bhagat. Optimization and validation of analytical conditions for bovine serum albumin using capillary electrophoresis. Anal. Biochem. 204:103-106 (1992).
    • (1992) Anal. Biochem. , vol.204 , pp. 103-106
    • Pande, P.G.1    Nellore, R.V.2    Bhagat, H.R.3
  • 16
    • 0028899753 scopus 로고
    • Hydrophobic surfaces that are hidden in chaperonin Cpn60 can be exposed by formation of assembly-competent monomers or by ionic perturbation of the oligomer
    • P.M. Horowitz, S. Hua, and D. L. Gibbons. Hydrophobic surfaces that are hidden in chaperonin Cpn60 can be exposed by formation of assembly-competent monomers or by ionic perturbation of the oligomer. J. Biol. Chem. 207:1535-1542 (1995).
    • (1995) J. Biol. Chem. , vol.207 , pp. 1535-1542
    • Horowitz, P.M.1    Hua, S.2    Gibbons, D.L.3
  • 17
    • 0034254742 scopus 로고    scopus 로고
    • Role of Arg-410 and Tyr-411 in human serum albumin for ligand binding and esterase-like activity
    • H. Watanabe, S. Tanase, K. Nakajou, T. Maruyama, U. Kragh-Hansen, and M. Otagiri. Role of Arg-410 and Tyr-411 in human serum albumin for ligand binding and esterase-like activity. Biochem. J. 349:813-819 (2000).
    • (2000) Biochem. J. , vol.349 , pp. 813-819
    • Watanabe, H.1    Tanase, S.2    Nakajou, K.3    Maruyama, T.4    Kragh-Hansen, U.5    Otagiri, M.6
  • 18
    • 0025148495 scopus 로고
    • Disposition characteristics of macromolecules in tumor-bearing mice
    • Y. Takakura, T. Fujita, M. Hashida, and H. Sezaki. Disposition characteristics of macromolecules in tumor-bearing mice. Pharm. Res. 7:339-346 (1990).
    • (1990) Pharm. Res. , vol.7 , pp. 339-346
    • Takakura, Y.1    Fujita, T.2    Hashida, M.3    Sezaki, H.4
  • 19
    • 0027368237 scopus 로고
    • Intracellular metabolism of indium-111-DTPA-labeled receptor targeted proteins
    • J.R. Duncan and M.J. Welch. Intracellular metabolism of indium-111-DTPA-labeled receptor targeted proteins. J. Nucl. Med. 34:1728-1738 (1993).
    • (1993) J. Nucl. Med. , vol.34 , pp. 1728-1738
    • Duncan, J.R.1    Welch, M.J.2
  • 20
    • 0019854279 scopus 로고
    • Pharmacokinetic analysis program (multi) for microcomputer
    • K. Yamaoka, Y. Tanigawara, T. Nakagawa, and T. Uno. Pharmacokinetic analysis program (multi) for microcomputer. J. Pharmacobiodyn. 4:879-885 (1981).
    • (1981) J. Pharmacobiodyn. , vol.4 , pp. 879-885
    • Yamaoka, K.1    Tanigawara, Y.2    Nakagawa, T.3    Uno, T.4
  • 21
    • 0033051066 scopus 로고    scopus 로고
    • In-vivo evaluation of indium-111-diethylenetriaminepentaacetic acid-labelling for determining the sites and rates of protein catabolism in mice
    • T. Mukai, Y. Arano, K. Nishida, H. Sasaki, H. Saji, and J. Nakamura. In-vivo evaluation of indium-111-diethylenetriaminepentaacetic acid-labelling for determining the sites and rates of protein catabolism in mice. J. Pharm. Pharmacol. 51:15-20 (1999).
    • (1999) J. Pharm. Pharmacol. , vol.51 , pp. 15-20
    • Mukai, T.1    Arano, Y.2    Nishida, K.3    Sasaki, H.4    Saji, H.5    Nakamura, J.6
  • 22
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • G. Sudlow, D. J. Birkett, and D. N. Wade. The characterization of two specific drug binding sites on human serum albumin. Mol. Pharmacol. 11:824-832 (1975).
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 24
    • 0032712774 scopus 로고    scopus 로고
    • Helix 6 of subdomain IIIA of human serum albumin is the region primarily photolabeled by ketoprofen, an arylpropionic acid NSAID containing a benzophenone moiety
    • V. T. G. Chuang, A. Kuniyasu, H. Nakayama, Y. Matsushita, S. Hirono, and M. Otagiri. Helix 6 of subdomain IIIA of human serum albumin is the region primarily photolabeled by ketoprofen, an arylpropionic acid NSAID containing a benzophenone moiety. Biochim. Biophys. Acta 1434:18-30 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1434 , pp. 18-30
    • Chuang, V.T.G.1    Kuniyasu, A.2    Nakayama, H.3    Matsushita, Y.4    Hirono, S.5    Otagiri, M.6
  • 25
    • 0035397254 scopus 로고    scopus 로고
    • Conformational stability and warfarin-binding properties of human serum albumin studied by recombinant mutants
    • H. Watanabe, U. Kragh-Hansen, S. Tanase, K. Nakajou, M. Mitarai, Y. Iwao, T. Maruyama, and M. Otagiri. Conformational stability and warfarin-binding properties of human serum albumin studied by recombinant mutants. Biochem. J. 357:269-274 (2001).
    • (2001) Biochem. J. , vol.357 , pp. 269-274
    • Watanabe, H.1    Kragh-Hansen, U.2    Tanase, S.3    Nakajou, K.4    Mitarai, M.5    Iwao, Y.6    Maruyama, T.7    Otagiri, M.8
  • 26
    • 0031050251 scopus 로고    scopus 로고
    • Advanced glycation end products are eliminated by scavenger-receptor-mediated endocytosis in hepatic sinusoidal, Kupffer and endothelial cells
    • B. Smedsrod, J. Melkko, N. Araki, H. Sano, and S. Horiuchi. Advanced glycation end products are eliminated by scavenger-receptor-mediated endocytosis in hepatic sinusoidal, Kupffer and endothelial cells. Biochem. J. 322:567-573 (1997).
    • (1997) Biochem. J. , vol.322 , pp. 567-573
    • Smedsrod, B.1    Melkko, J.2    Araki, N.3    Sano, H.4    Horiuchi, S.5


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