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Volumn 474, Issue , 2010, Pages 181-195

Redox State of Human Serum Albumin in Terms of Cysteine-34 in Health and Disease

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; SERUM ALBUMIN;

EID: 79958070517     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)74011-8     Document Type: Chapter
Times cited : (97)

References (34)
  • 1
    • 0014030335 scopus 로고
    • The heterogeneity of bovine serum albumin
    • Anderson, L.O., The heterogeneity of bovine serum albumin. Biochim. Biophys. Acta 117 (1965), 115–133.
    • (1965) Biochim. Biophys. Acta , vol.117 , pp. 115-133
    • Anderson, L.O.1
  • 4
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • Curry, S., Mandelkow, H., Brick, P., Franks, N., Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat. Struct. Biol. 5 (1998), 827–835.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.4
  • 5
    • 0036977353 scopus 로고    scopus 로고
    • Aging-related changes in the thiol/disulfide redox state: Implication for the use of thiol antioxidants
    • Dröge, W., Aging-related changes in the thiol/disulfide redox state: Implication for the use of thiol antioxidants. Exp. Gerontol. 37 (2002), 1331–1343.
    • (2002) Exp. Gerontol. , vol.37 , pp. 1331-1343
    • Dröge, W.1
  • 6
    • 0023881390 scopus 로고
    • Further studies on the resolution of human mercapt- and nonmercaptalbumin and on human serum albumin in the elderly by high-performance liquid chromatography
    • Era, S., Hamaguchi, T., Sogami, M., Kuwata, K., Suzuki, E., Miura, K., Kawai, K., Kitazawa, Y., Okabe, H., Noma, A., Miyata, S., Further studies on the resolution of human mercapt- and nonmercaptalbumin and on human serum albumin in the elderly by high-performance liquid chromatography. Int. J. Pept. Protein Res. 31 (1988), 435–442.
    • (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
  • 8
    • 0003536299 scopus 로고    scopus 로고
    • Free Radicals in Biology and Medicine
    • Oxford University Press New York
    • Halliwell, B., Gutteridge, J.M.C., Free Radicals in Biology and Medicine. 1999, Oxford University Press, New York.
    • (1999)
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 9
    • 16644398454 scopus 로고    scopus 로고
    • Kinetic studies of covalent binding between N-acetyl-L-cysteine and human serum albumin through a mixed-disulfide using an N-methylpyridinium polymer-based column
    • Harada, D., Anraku, M., Fukuda, H., Naito, S., Harada, K., Suenaga, A., Otagiri, M., Kinetic studies of covalent binding between N-acetyl-L-cysteine and human serum albumin through a mixed-disulfide using an N-methylpyridinium polymer-based column. Drug Metab. Pharmacokin. 19 (2004), 297–302.
    • (2004) Drug Metab. Pharmacokin. , vol.19 , pp. 297-302
    • Harada, D.1    Anraku, M.2    Fukuda, H.3    Naito, S.4    Harada, K.5    Suenaga, A.6    Otagiri, M.7
  • 10
    • 0033958443 scopus 로고    scopus 로고
    • Observation for redox state of human serum and aqueous humor albumin from patients with senile cataract
    • Hayashi, T., Era, S., Kawai, K., Imai, H., Nakamura, K., Onda, E., Yoh, M., Observation for redox state of human serum and aqueous humor albumin from patients with senile cataract. Pathophysiology 6 (2000), 237–243.
    • (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
  • 11
    • 0036135316 scopus 로고    scopus 로고
    • The importance of sample preservation temperature for analysis of the redox state of human serum albumin
    • Hayashi, T., Imai, H., Kuwata, K., Sogami, M., Era, S., The importance of sample preservation temperature for analysis of the redox state of human serum albumin. Clin. Chim. Acta 316 (2002), 175–178.
    • (2002) Clin. Chim. Acta , vol.316 , pp. 175-178
    • Hayashi, T.1    Imai, H.2    Kuwata, K.3    Sogami, M.4    Era, S.5
  • 12
    • 0037172351 scopus 로고    scopus 로고
    • Simple and sensitive high-performance liquid chromatographic method for the investigation of dynamic chances in the redox state of rat serum albumin
    • Hayashi, T., Suda, K., Imai, H., Era, S., Simple and sensitive high-performance liquid chromatographic method for the investigation of dynamic chances in the redox state of rat serum albumin. J. Chromatogr. B 772 (2002), 139–146.
    • (2002) J. Chromatogr. B , vol.772 , pp. 139-146
    • Hayashi, T.1    Suda, K.2    Imai, H.3    Era, S.4
  • 13
    • 0034951428 scopus 로고    scopus 로고
    • Albumin is the major plasma protein target of oxidant stress in uremia
    • Himmelfarb, J., McMonagle, E., Albumin is the major plasma protein target of oxidant stress in uremia. Kidney Int. 60 (2001), 358–363.
    • (2001) Kidney Int. , vol.60 , pp. 358-363
    • Himmelfarb, J.1    McMonagle, E.2
  • 16
    • 0014409423 scopus 로고
    • The heterogeneity of bovine albumin with respect to sulfhydryl and dimer content
    • Janatova, J., Fuller, J.K., Hunter, M.J., The heterogeneity of bovine albumin with respect to sulfhydryl and dimer content. J. Biol. Chem. 243 (1968), 3612–3622.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3612-3622
    • Janatova, J.1    Fuller, J.K.2    Hunter, M.J.3
  • 17
    • 0036829579 scopus 로고    scopus 로고
    • Redox analysis of human plasma allows separation of pro-oxidant events of aging from decline in antioxidant defenses
    • Jones, D.P., Mody, V.C., Carlson, J.L., Lynn, M.J., Sternberg, P., Redox analysis of human plasma allows separation of pro-oxidant events of aging from decline in antioxidant defenses. Free Radic. Biol. Med. 33 (2002), 1290–1300.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1290-1300
    • Jones, D.P.1    Mody, V.C.2    Carlson, J.L.3    Lynn, M.J.4    Sternberg, P.5
  • 18
    • 49649089510 scopus 로고    scopus 로고
    • Single bouts of exercise affect albumin redox state and carbonyl groups on plasma protein of trained men in a workload-dependent manner
    • Lamprecht, M., Greilberger, J.F., Schwaberger, G., Hofmann, P., Oettl, K., Single bouts of exercise affect albumin redox state and carbonyl groups on plasma protein of trained men in a workload-dependent manner. J. Appl. Physiol. 104 (2008), 1611–1617.
    • (2008) J. Appl. Physiol. , vol.104 , pp. 1611-1617
    • Lamprecht, M.1    Greilberger, J.F.2    Schwaberger, G.3    Hofmann, P.4    Oettl, K.5
  • 22
    • 68749120642 scopus 로고    scopus 로고
    • Albumin thiol oxidation and serum protein carbonyl formation are progressively enhanced with advancing stages of chronic kidney disease
    • Matsuyama, Y., Terawaki, H., Terada, T., Era, S., Albumin thiol oxidation and serum protein carbonyl formation are progressively enhanced with advancing stages of chronic kidney disease. Clin. Exp.Nephrol. 13 (2009), 308–315.
    • (2009) Clin. Exp.Nephrol. , vol.13 , pp. 308-315
    • Matsuyama, Y.1    Terawaki, H.2    Terada, T.3    Era, S.4
  • 23
    • 34347324020 scopus 로고    scopus 로고
    • Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties
    • Oettl, K., Stauber, R.E., Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties. Br. J. Pharmacol. 151 (2007), 580–590.
    • (2007) Br. J. Pharmacol. , vol.151 , pp. 580-590
    • Oettl, K.1    Stauber, R.E.2
  • 25
    • 70349782867 scopus 로고    scopus 로고
    • Effect of extracorporeal liver support by molecular adsorbents recirculating system and prometheus on redox state of albumin in acute-on-chronic liver failure
    • Oettl, K., Stadlbauer, V., Krisper, P., Stauber, R.E., Effect of extracorporeal liver support by molecular adsorbents recirculating system and prometheus on redox state of albumin in acute-on-chronic liver failure. Ther. Apher. Dial. 13 (2009), 431–436.
    • (2009) Ther. Apher. Dial. , vol.13 , pp. 431-436
    • Oettl, K.1    Stadlbauer, V.2    Krisper, P.3    Stauber, R.E.4
  • 26
    • 79952213460 scopus 로고    scopus 로고
    • The redox state of human serum albumin in eye diseases with and without complications
    • doi: 10.1111/j.1755-3768.2009.01824.x
    • Oettl, K., Reibnegger, G., Schmut, O., The redox state of human serum albumin in eye diseases with and without complications. Acta Ophthalmol., 2010 doi: 10.1111/j.1755-3768.2009.01824.x.
    • (2010) Acta Ophthalmol.
    • Oettl, K.1    Reibnegger, G.2    Schmut, O.3
  • 27
    • 0003626648 scopus 로고    scopus 로고
    • All About Albumin; Biochemistry, Genetics and Medical Applications
    • Academic Press San Diego, CA
    • Peters, T., All About Albumin; Biochemistry, Genetics and Medical Applications. 1996, Academic Press, San Diego, CA.
    • (1996)
    • Peters, T.1
  • 28
    • 0028143826 scopus 로고
    • Differential susceptibility of plasma proteins to oxidative modification: examination by western blot immunoassay
    • Shacter, E., Williams, J.A., Lim, M., Levine, R.L., Differential susceptibility of plasma proteins to oxidative modification: examination by western blot immunoassay. Free Radic. Biol. Med. 17 (1994), 429–437.
    • (1994) Free Radic. Biol. Med. , vol.17 , pp. 429-437
    • Shacter, E.1    Williams, J.A.2    Lim, M.3    Levine, R.L.4
  • 33
    • 1342325627 scopus 로고    scopus 로고
    • The redox states of serum and synovial fluid of patients with temporomandibular joint disorders
    • Tomida, M., Ishimaru, J.I., Hayashi, T., Nakamura, K., Murayama, K., Era, S., The redox states of serum and synovial fluid of patients with temporomandibular joint disorders. Jpn. J. Physiol. 53 (2003), 351–355.
    • (2003) Jpn. J. Physiol. , vol.53 , pp. 351-355
    • Tomida, M.1    Ishimaru, J.I.2    Hayashi, T.3    Nakamura, K.4    Murayama, K.5    Era, S.6
  • 34
    • 70249137283 scopus 로고    scopus 로고
    • Sulfenic acid—A key intermediate in albumin thiol oxidation
    • Turell, L., Botti, H., Carballal, S., Radi, R., Alvarez, B., Sulfenic acid—A key intermediate in albumin thiol oxidation. J. Chromatogr. B 877 (2009), 3384–3392.
    • (2009) J. Chromatogr. B , vol.877 , pp. 3384-3392
    • Turell, L.1    Botti, H.2    Carballal, S.3    Radi, R.4    Alvarez, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.