메뉴 건너뛰기




Volumn 90, Issue 3, 2008, Pages 170-178

Effect of UVC radiation on conformational restructuring of human serum albumin

Author keywords

Differential scanning calorimetry; Human serum albumin; UVC radiation

Indexed keywords

HUMAN SERUM ALBUMIN;

EID: 40749135789     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2007.12.007     Document Type: Article
Times cited : (28)

References (43)
  • 2
    • 0035182390 scopus 로고    scopus 로고
    • Ultraviolet light induced injury: immunological and inflammatory effects
    • Clydesdale J., Dandie G.W., and Muller H.K. Ultraviolet light induced injury: immunological and inflammatory effects. Immunol. Cell. Biol. 79 (2001) 547-568
    • (2001) Immunol. Cell. Biol. , vol.79 , pp. 547-568
    • Clydesdale, J.1    Dandie, G.W.2    Muller, H.K.3
  • 3
    • 40749125463 scopus 로고    scopus 로고
    • National Radiological Protection Board, Health effect from ultraviolet radiation, Report of an Advisory Group on Non-ionising Radiation, Documents of the NRPB 13, 2002, pp. 1-292; http://www.hpa.org.uk/radiation/publications/documents_of_nrpb/pdfs/doc_13_1.pdf (02.11.2007).
    • National Radiological Protection Board, Health effect from ultraviolet radiation, Report of an Advisory Group on Non-ionising Radiation, Documents of the NRPB 13, 2002, pp. 1-292; http://www.hpa.org.uk/radiation/publications/documents_of_nrpb/pdfs/doc_13_1.pdf (02.11.2007).
  • 4
    • 0031679944 scopus 로고    scopus 로고
    • Changes in serum levels of sialo-glycoproteins in mice exposed to UVB radiation
    • Yamamoto K., Furuya T., Kameoka Y., and Kawanaka M. Changes in serum levels of sialo-glycoproteins in mice exposed to UVB radiation. Biol. Pharm. Bull. 21 (1998) 1000-1002
    • (1998) Biol. Pharm. Bull. , vol.21 , pp. 1000-1002
    • Yamamoto, K.1    Furuya, T.2    Kameoka, Y.3    Kawanaka, M.4
  • 5
    • 13844298316 scopus 로고    scopus 로고
    • Effect of UVB radiation on human erythrocytes in vitro
    • Misra R.B., Ray R.S., and Hans R.K. Effect of UVB radiation on human erythrocytes in vitro. Toxicol. in Vitro 19 (2005) 433-438
    • (2005) Toxicol. in Vitro , vol.19 , pp. 433-438
    • Misra, R.B.1    Ray, R.S.2    Hans, R.K.3
  • 6
    • 13444260366 scopus 로고    scopus 로고
    • Vacuum-UV-radiation-induced structural - functional changes in serum albumin molecules
    • Artyukhov V.G., Pantyavin A.A., and Vashanov G.A. Vacuum-UV-radiation-induced structural - functional changes in serum albumin molecules. J. Appl. Spectrosc. 68 (2001) 291-298
    • (2001) J. Appl. Spectrosc. , vol.68 , pp. 291-298
    • Artyukhov, V.G.1    Pantyavin, A.A.2    Vashanov, G.A.3
  • 7
    • 0033103067 scopus 로고    scopus 로고
    • UV-B-induced secondary conformational changes in lens α-crystallin
    • Lin S.Y., Cho Ch.J., and Li M.J. UV-B-induced secondary conformational changes in lens α-crystallin. J. Photochem. Photobiol. 49 (1999) 29-34
    • (1999) J. Photochem. Photobiol. , vol.49 , pp. 29-34
    • Lin, S.Y.1    Cho, Ch.J.2    Li, M.J.3
  • 8
    • 13444258081 scopus 로고    scopus 로고
    • Thermal stability of bovine serum albumin exposed to the action of UV radiation
    • Michnik A., and Michalik K. Thermal stability of bovine serum albumin exposed to the action of UV radiation. Phys. Med. XX Suppl. 1 (2004) 111-113
    • (2004) Phys. Med. , vol.XX , Issue.SUPPL. 1 , pp. 111-113
    • Michnik, A.1    Michalik, K.2
  • 9
    • 2442696753 scopus 로고    scopus 로고
    • Hair color changes and protein damage caused by ultraviolet radiation
    • Santos Nogueira A.C., and Joekes I. Hair color changes and protein damage caused by ultraviolet radiation. J. Photochem. Photobiol. 74 (2004) 109-117
    • (2004) J. Photochem. Photobiol. , vol.74 , pp. 109-117
    • Santos Nogueira, A.C.1    Joekes, I.2
  • 10
    • 0026184912 scopus 로고
    • Effect of cysteine on bovine serum albumin (BSA) denaturation induced by solar ultraviolet (UVA, UVB) irradiation
    • Watanabe Y., Horii I., Nakayama Y., and Osawa T. Effect of cysteine on bovine serum albumin (BSA) denaturation induced by solar ultraviolet (UVA, UVB) irradiation. Chem. Pharm. Bull. 39 (1991) 1796-1801
    • (1991) Chem. Pharm. Bull. , vol.39 , pp. 1796-1801
    • Watanabe, Y.1    Horii, I.2    Nakayama, Y.3    Osawa, T.4
  • 11
    • 0023655531 scopus 로고
    • Protein damage and degradation by oxygen radicals III. Modification of secondary and tertiary structure
    • Davies K.J.A., and Delsignore M.E. Protein damage and degradation by oxygen radicals III. Modification of secondary and tertiary structure. J. Biol. Chem. 262 (1987) 9908-9913
    • (1987) J. Biol. Chem. , vol.262 , pp. 9908-9913
    • Davies, K.J.A.1    Delsignore, M.E.2
  • 14
    • 20444370296 scopus 로고    scopus 로고
    • Design of a UV-C irradiation process for the inactivation of viruses in protein solutions
    • Li Q., MacDonald S., Bienek C., Foster P.R., and MacLeod A.J. Design of a UV-C irradiation process for the inactivation of viruses in protein solutions. Biologicals 33 (2005) 101-110
    • (2005) Biologicals , vol.33 , pp. 101-110
    • Li, Q.1    MacDonald, S.2    Bienek, C.3    Foster, P.R.4    MacLeod, A.J.5
  • 15
    • 1842735647 scopus 로고    scopus 로고
    • Continuous-flow UVC irradiation: a new, effective, protein activity-preserving system for inactivating bacteria and viruses, including erythrovirus B19
    • Caillet-Fauquet P., Di Giambattista M., Draps M.L., Sandras F., Branckaert T., de Launoit Y., and Laub R. Continuous-flow UVC irradiation: a new, effective, protein activity-preserving system for inactivating bacteria and viruses, including erythrovirus B19. J. Virol. Meth. 118 (2004) 131-139
    • (2004) J. Virol. Meth. , vol.118 , pp. 131-139
    • Caillet-Fauquet, P.1    Di Giambattista, M.2    Draps, M.L.3    Sandras, F.4    Branckaert, T.5    de Launoit, Y.6    Laub, R.7
  • 16
    • 33750171095 scopus 로고    scopus 로고
    • Study of the interaction of artemisinin with bovine serum albumin
    • Bian H., Li M., Yu Q., Chen Z., Tian J., and Liang H. Study of the interaction of artemisinin with bovine serum albumin. Int. J. Biol. Macromol. 39 (2006) 291-297
    • (2006) Int. J. Biol. Macromol. , vol.39 , pp. 291-297
    • Bian, H.1    Li, M.2    Yu, Q.3    Chen, Z.4    Tian, J.5    Liang, H.6
  • 17
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He X.M., and Carter D.C. Atomic structure and chemistry of human serum albumin. Nature 358 (1992) 209-215
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 18
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter D.C., and Ho J.X. Structure of serum albumin. Adv. Prot. Chem. 45 (1994) 153-203
    • (1994) Adv. Prot. Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 19
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • Curry S., Mandelkov H., Brick P., and Franks N.P. 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    Mandelkov, H.2    Brick, P.3    Franks, N.P.4
  • 20
    • 0032720125 scopus 로고    scopus 로고
    • Fatty acid binding to human serum albumin: new insight from crystallographic studies
    • Curry S., Brick P., and Franks N.P. Fatty acid binding to human serum albumin: new insight from crystallographic studies. Biochim. Biophys. Acta 1441 (1999) 131-140
    • (1999) Biochim. Biophys. Acta , vol.1441 , pp. 131-140
    • Curry, S.1    Brick, P.2    Franks, N.P.3
  • 21
    • 0033062612 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin at 2.5 Å resolutions
    • Sugio S., Kashima A., Mochizuki S., Noda M., and Kobayashi K. Crystal structure of human serum albumin at 2.5 Å resolutions. Protein Eng. 12 (1999) 439-446
    • (1999) Protein Eng. , vol.12 , pp. 439-446
    • Sugio, S.1    Kashima, A.2    Mochizuki, S.3    Noda, M.4    Kobayashi, K.5
  • 22
    • 0034634370 scopus 로고    scopus 로고
    • Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin
    • Bhattacharya A.A., Grune T., and Curry S. Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. J. Mol. Biol. 303 (2000) 721-732
    • (2000) J. Mol. Biol. , vol.303 , pp. 721-732
    • Bhattacharya, A.A.1    Grune, T.2    Curry, S.3
  • 23
    • 0035861982 scopus 로고    scopus 로고
    • Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids
    • Petitpas I., Grune T., Bhattacharya A.A., and Curry S. Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids. J. Mol. Biol. 314 (2001) 955-960
    • (2001) J. Mol. Biol. , vol.314 , pp. 955-960
    • Petitpas, I.1    Grune, T.2    Bhattacharya, A.A.3    Curry, S.4
  • 24
    • 21744445084 scopus 로고    scopus 로고
    • A molecular dynamic study of human serum albumin binding sites
    • Artali R., Bombieri G., Calabi L., and Delpra A. A molecular dynamic study of human serum albumin binding sites. II Farmaco 60 (2005) 485-495
    • (2005) II Farmaco , vol.60 , pp. 485-495
    • Artali, R.1    Bombieri, G.2    Calabi, L.3    Delpra, A.4
  • 25
    • 0023746489 scopus 로고
    • Decrease in stability of human albumin with increase in protein concentration
    • Ross P.D., and Shrake A. Decrease in stability of human albumin with increase in protein concentration. J. Biol. Chem. 263 (1988) 11196-11202
    • (1988) J. Biol. Chem. , vol.263 , pp. 11196-11202
    • Ross, P.D.1    Shrake, A.2
  • 26
    • 0023696943 scopus 로고
    • Biphasic denaturation of human albumin due to ligand redistribution during unfolding
    • Shrake A., and Ross P.D. Biphasic denaturation of human albumin due to ligand redistribution during unfolding. J. Biol. Chem. 263 (1988) 15392-15399
    • (1988) J. Biol. Chem. , vol.263 , pp. 15392-15399
    • Shrake, A.1    Ross, P.D.2
  • 28
    • 0031896612 scopus 로고    scopus 로고
    • Species differences of serum albumins II. Chemical and thermal stability
    • Kosa T., Maruyama T., and Otagiri M. Species differences of serum albumins II. Chemical and thermal stability. Pharm. Res. 15 (1998) 449-454
    • (1998) Pharm. Res. , vol.15 , pp. 449-454
    • Kosa, T.1    Maruyama, T.2    Otagiri, M.3
  • 29
    • 0033730129 scopus 로고    scopus 로고
    • Differential scanning calorimetry of albumin solders: interspecies differences and fatty acid binding effects on protein denaturation
    • Bleustein C.B., Sennett M., Kung R.T.V., Felsen D., Poppas P., and Stewart R.B. Differential scanning calorimetry of albumin solders: interspecies differences and fatty acid binding effects on protein denaturation. Lasers Surg. Med. 27 (2000) 465-470
    • (2000) Lasers Surg. Med. , vol.27 , pp. 465-470
    • Bleustein, C.B.1    Sennett, M.2    Kung, R.T.V.3    Felsen, D.4    Poppas, P.5    Stewart, R.B.6
  • 30
    • 0037289151 scopus 로고    scopus 로고
    • Thermal stability of bovine serum albumin DSC study
    • Michnik A. Thermal stability of bovine serum albumin DSC study. J. Therm. Anal. Cal. 71 (2003) 509-519
    • (2003) J. Therm. Anal. Cal. , vol.71 , pp. 509-519
    • Michnik, A.1
  • 32
    • 0033854283 scopus 로고    scopus 로고
    • Welding characteristics of different albumin species with and without fatty acids
    • Bleustein C.B., Felsen D., and Poppas P. Welding characteristics of different albumin species with and without fatty acids. Lasers Surg. Med. 27 (2000) 82-86
    • (2000) Lasers Surg. Med. , vol.27 , pp. 82-86
    • Bleustein, C.B.1    Felsen, D.2    Poppas, P.3
  • 33
    • 0025046965 scopus 로고
    • Differential scanning calorimetric studies on bovine serum albumin: I. Effects of pH and ionic strength
    • Yamasaki M., Yano H., and Aoki K. Differential scanning calorimetric studies on bovine serum albumin: I. Effects of pH and ionic strength. Int. J. Biol. Macromol. 12 (1990) 263-268
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 263-268
    • Yamasaki, M.1    Yano, H.2    Aoki, K.3
  • 34
    • 0035400013 scopus 로고    scopus 로고
    • Osmotic pressure, small-angle X-ray, and dynamic light scattering studies of human serum albumin in aqueous solutions
    • Rešcič J., Vlachy V., Jamnik A., and Glatter O. Osmotic pressure, small-angle X-ray, and dynamic light scattering studies of human serum albumin in aqueous solutions. J. Coll. Int. Science 239 (2001) 49-57
    • (2001) J. Coll. Int. Science , vol.239 , pp. 49-57
    • Rešcič, J.1    Vlachy, V.2    Jamnik, A.3    Glatter, O.4
  • 35
    • 34248155667 scopus 로고    scopus 로고
    • Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity
    • Supporting information
    • Lindman S., Lynch I., Thulin E., Nilsson H., Dawson K.A., and Linse S. Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity. Nano Lett. 7 (2007) 914-920 Supporting information
    • (2007) Nano Lett. , vol.7 , pp. 914-920
    • Lindman, S.1    Lynch, I.2    Thulin, E.3    Nilsson, H.4    Dawson, K.A.5    Linse, S.6
  • 36
  • 37
    • 34248572429 scopus 로고    scopus 로고
    • Effect of ethanol on the thermal stability of human serum albumin
    • Michnik A., and Drzazga Z. Effect of ethanol on the thermal stability of human serum albumin. J. Therm. Anal. Cal. 88 2 (2007) 449-454
    • (2007) J. Therm. Anal. Cal. , vol.88 , Issue.2 , pp. 449-454
    • Michnik, A.1    Drzazga, Z.2
  • 38
    • 0029148319 scopus 로고
    • Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis
    • van Stokkum I.H.M., Linsdell H., Hadden J.M., Hais P.I., Chapman D., and Bloemendal M. Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis. Biochemistry 34 (1995) 10508-10518
    • (1995) Biochemistry , vol.34 , pp. 10508-10518
    • van Stokkum, I.H.M.1    Linsdell, H.2    Hadden, J.M.3    Hais, P.I.4    Chapman, D.5    Bloemendal, M.6
  • 39
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill K.A. Dominant forces in protein folding. Biochemistry 29 (1990) 7133-7155
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 40
    • 0025098571 scopus 로고
    • Common features of protein unfolding and dissolution of hydrophobic compounds
    • Murphy K.P., Privalov P.L., and Gill S.J. Common features of protein unfolding and dissolution of hydrophobic compounds. Science 247 (1990) 559-561
    • (1990) Science , vol.247 , pp. 559-561
    • Murphy, K.P.1    Privalov, P.L.2    Gill, S.J.3
  • 41
    • 0034971963 scopus 로고    scopus 로고
    • Heat capacity changes upon burial of polar and non-polar groups in proteins
    • Loladze V.V., Ermolenko D.N., and Makhatadze G.I. Heat capacity changes upon burial of polar and non-polar groups in proteins. Protein Sci. 10 (2001) 1343-1352
    • (2001) Protein Sci. , vol.10 , pp. 1343-1352
    • Loladze, V.V.1    Ermolenko, D.N.2    Makhatadze, G.I.3
  • 42
    • 0026344361 scopus 로고
    • Solid model compounds and the thermodynamics of protein unfolding
    • Murphy K.P., and Gill S.J. Solid model compounds and the thermodynamics of protein unfolding. J. Mol. Biol. 222 (1991) 699-709
    • (1991) J. Mol. Biol. , vol.222 , pp. 699-709
    • Murphy, K.P.1    Gill, S.J.2
  • 43
    • 0029860343 scopus 로고    scopus 로고
    • Water mediated protein-DNA interactions: the relationship of thermodynamics to structural detail
    • Morton C.J., and Ladbury J.E. Water mediated protein-DNA interactions: the relationship of thermodynamics to structural detail. Protein Sci. 5 (1996) 2115-2118
    • (1996) Protein Sci. , vol.5 , pp. 2115-2118
    • Morton, C.J.1    Ladbury, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.