메뉴 건너뛰기




Volumn 17, Issue 1, 2006, Pages 146-151

Human serum albumin hybrid incorporating tailed porphyrinatoiron(II) in the α,α,α,β-conformer as an O2-binding site

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BLOOD; CELLS; HEMOGLOBIN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RATE CONSTANTS;

EID: 31544455290     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc050154+     Document Type: Article
Times cited : (11)

References (28)
  • 1
    • 1542334754 scopus 로고    scopus 로고
    • Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin
    • (a) Collman, J. P., Boulatov, R., Sunderland, C. J., and Fu, L. (2004) Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin. Chem. Rev. 104, 561-588.
    • (2004) Chem. Rev. , vol.104 , pp. 561-588
    • Collman, J.P.1    Boulatov, R.2    Sunderland, C.J.3    Fu, L.4
  • 2
    • 3042907629 scopus 로고
    • Synthetic heme-dioxygen complexes
    • and references therein
    • (b) Momenteau, M., and Reed, C. A. (1994) Synthetic heme-dioxygen complexes. Chem. Rev. 94, 659-698 and references therein.
    • (1994) Chem. Rev. , vol.94 , pp. 659-698
    • Momenteau, M.1    Reed, C.A.2
  • 4
    • 0037011054 scopus 로고    scopus 로고
    • Self-organized lipid-porphyrin bilayer membranes in vesicular form: Nanostructure, photophysical properties and dioxygen coordination
    • Komatsu, T., Moritake, M., Nakagawa, A., and Tsuchida, E. (2002) Self-organized lipid-porphyrin bilayer membranes in vesicular form: Nanostructure, photophysical properties and dioxygen coordination. Chem. Eur. J. 8, 5469-5480.
    • (2002) Chem. Eur. J. , vol.8 , pp. 5469-5480
    • Komatsu, T.1    Moritake, M.2    Nakagawa, A.3    Tsuchida, E.4
  • 5
    • 7744228408 scopus 로고    scopus 로고
    • Physicochemical characterization of cross-linked human serum albumin dimer and its synthetic heme hybrid as an oxygen carrier
    • Komatsu, T., Oguro, Y., Teramura, Y., Takeoka, S., Okai, J., Anraku, M., Otagiri, M., and Tsuchida, E. (2004) Physicochemical characterization of cross-linked human serum albumin dimer and its synthetic heme hybrid as an oxygen carrier. Biochim. Biophys. Acta 1675, 21-31.
    • (2004) Biochim. Biophys. Acta , vol.1675 , pp. 21-31
    • Komatsu, T.1    Oguro, Y.2    Teramura, Y.3    Takeoka, S.4    Okai, J.5    Anraku, M.6    Otagiri, M.7    Tsuchida, E.8
  • 7
    • 9644276913 scopus 로고    scopus 로고
    • Exchange transfusion with synthetic oxygen-carrying plasma protein "albumin-heme" into an acute anemia rat model after seventy-percent hemodilution
    • (b) Komatsu, T., Huang, Y., Yamamoto, H., Horinouchi, H., Kobayashi, K., and Tsuchida, E. (2004) Exchange transfusion with synthetic oxygen-carrying plasma protein "albumin-heme" into an acute anemia rat model after seventy-percent hemodilution. J. Biomed. Mater. Res. 71A, 644-651.
    • (2004) J. Biomed. Mater. Res. , vol.71 A , pp. 644-651
    • Komatsu, T.1    Huang, Y.2    Yamamoto, H.3    Horinouchi, H.4    Kobayashi, K.5    Tsuchida, E.6
  • 8
    • 4544344911 scopus 로고    scopus 로고
    • Exchange transfusion with entirely synthetic red-cell substitute albumin-heme into rats: Physiological responses and blood biochemical tests
    • Huang, Y., Komatsu, T., Yamamoto, H., Horinouchi, H., Kobayashi. K., and Tsuchida, E. (2004) Exchange transfusion with entirely synthetic red-cell substitute albumin-heme into rats: physiological responses and blood biochemical tests. J. Biomed. Mater. Res. 71A, 63-69.
    • (2004) J. Biomed. Mater. Res. , vol.71 A , pp. 63-69
    • Huang, Y.1    Komatsu, T.2    Yamamoto, H.3    Horinouchi, H.4    Kobayashi, K.5    Tsuchida, E.6
  • 10
    • 33847086185 scopus 로고
    • Increased yield of a desired isomer by equilibriums displacement on binding to silica gel, applied to mesotetrakis(o-aminophenyl)porphyrin
    • Lindsey, J. (1980) Increased yield of a desired isomer by equilibriums displacement on binding to silica gel, applied to mesotetrakis(o-aminophenyl) porphyrin. J. Org. Chem. 45, 5215-5215.
    • (1980) J. Org. Chem. , vol.45 , pp. 5215-5215
    • Lindsey, J.1
  • 12
    • 0006122996 scopus 로고
    • Synthesis and coordination behaviors of new double-sided porphyrinatoiron(II) complexes: Effect of the pocket size for imidazole on dioxygen binding
    • Tsuchida, E., Hasegawa, E., Komatsu, T., Nakata, T., Nakao, K., and Nishide, H. (1991) Synthesis and coordination behaviors of new double-sided porphyrinatoiron(II) complexes: effect of the pocket size for imidazole on dioxygen binding. Bull, Chem. Soc. Jpn. 64, 888-894.
    • (1991) Bull, Chem. Soc. Jpn. , vol.64 , pp. 888-894
    • Tsuchida, E.1    Hasegawa, E.2    Komatsu, T.3    Nakata, T.4    Nakao, K.5    Nishide, H.6
  • 13
    • 0032589975 scopus 로고    scopus 로고
    • 2-coordination structure of human serum albumin incorporating tetrakis-(o-pivalamido) phenylporphyrinatoiron(II) derivatives
    • 2-coordination structure of human serum albumin incorporating tetrakis-(o-pivalamido)phenylporphyrinatoiron(II) derivatives. Bioconjugate Chem. 10, 82-86.
    • (1999) Bioconjugate Chem. , vol.10 , pp. 82-86
    • Komatsu, T.1    Hamamatsu, K.2    Wu, J.3    Tsuchida, E.4
  • 14
    • 37049074485 scopus 로고
    • 2-binding properties of tetraphenylporphyrinatoiron(II) derivatives bearing a proximal imidazole covalently bound at the β-pyrrolic position
    • 2-binding properties of tetraphenylporphyrinatoiron(II) derivatives bearing a proximal imidazole covalently bound at the β-pyrrolic position. J. Chem. Soc., Perkin Trans. 2. 747-753.
    • (1995) J. Chem. Soc., Perkin Trans. 2 , pp. 747-753
    • Tsuchida, E.1    Komatsu, T.2    Kumamoto, S.3    Ando, K.4    Nishide, H.5
  • 17
    • 0032514845 scopus 로고    scopus 로고
    • Novel protecting strategy for the synthesis of porphyrins with different distal and proximal superstructures
    • Collman, J. P., Broring, M., Fu, L., Rapta, M., Schwenninger, R., and Straumanis, A. (1998) Novel protecting strategy for the synthesis of porphyrins with different distal and proximal superstructures. J. Org. Chem. 63, 8082-8083.
    • (1998) J. Org. Chem. , vol.63 , pp. 8082-8083
    • Collman, J.P.1    Broring, M.2    Fu, L.3    Rapta, M.4    Schwenninger, R.5    Straumanis, A.6
  • 18
    • 1542268903 scopus 로고    scopus 로고
    • Synthesis of a complementary dimer from mono(imidazolyl)-substituted cobalt(II) porhyrin as a new artificial T-form hemoglobin
    • Inaba, Y., and Kobuke, Y. (2004) Synthesis of a complementary dimer from mono(imidazolyl)-substituted cobalt(II) porhyrin as a new artificial T-form hemoglobin. Tetrahedron 60, 3097-3107.
    • (2004) Tetrahedron , vol.60 , pp. 3097-3107
    • Inaba, Y.1    Kobuke, Y.2
  • 19
    • 0001064211 scopus 로고
    • Hydrogen-bonded oxyhemoglobin models with substituted picket-fence porphyrins: The model compound equivalent of site-directed mutagenesis
    • Wuenschell, G. E., Tetreau, C., Lavalette, D., and Reed, C. A. (1992) Hydrogen-bonded oxyhemoglobin models with substituted picket-fence porphyrins: the model compound equivalent of site-directed mutagenesis. J. Am. Chem. Soc. 114, 3346-3355.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3346-3355
    • Wuenschell, G.E.1    Tetreau, C.2    Lavalette, D.3    Reed, C.A.4
  • 20
    • 0037155994 scopus 로고    scopus 로고
    • Biomimetic studies of terminal oxidases: Trisimidazole picket metalloporphyrins
    • Collman, J. P., Sunderland, C. J., and Boulatov, R. (2002) Biomimetic studies of terminal oxidases: trisimidazole picket metalloporphyrins. Inorg. Chem. 41, 2282-2291.
    • (2002) Inorg. Chem. , vol.41 , pp. 2282-2291
    • Collman, J.P.1    Sunderland, C.J.2    Boulatov, R.3
  • 21
    • 3042673067 scopus 로고    scopus 로고
    • Crystal structural analysis of human serum albumin complexes with hemin and fatty acid
    • Zunszain, P. A., Ghuman, J., Komatsu, T., Tsuchida, E., and Curry, S. (2003) Crystal structural analysis of human serum albumin complexes with hemin and fatty acid, BMC Struct. Biol. 3, 6.
    • (2003) BMC Struct. Biol. , vol.3 , pp. 6
    • Zunszain, P.A.1    Ghuman, J.2    Komatsu, T.3    Tsuchida, E.4    Curry, S.5
  • 22
    • 0025121488 scopus 로고
    • Binding of porphyrin to human serum albumin, structure-activity relationship
    • Cohen, S., and Margalit, R. (1990) Binding of porphyrin to human serum albumin, structure-activity relationship. Biochem. J. 270, 325-330.
    • (1990) Biochem. J. , vol.270 , pp. 325-330
    • Cohen, S.1    Margalit, R.2
  • 23
    • 0036198482 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction of a water soluble porphyrin and two drug carrier proteins
    • Andrade, S. M., and Costa, S. M. B. (2002) Spectroscopic studies on the interaction of a water soluble porphyrin and two drug carrier proteins. Biophys. J. 82, 1607-1619.
    • (2002) Biophys. J. , vol.82 , pp. 1607-1619
    • Andrade, S.M.1    Costa, S.M.B.2
  • 24
    • 0041366813 scopus 로고    scopus 로고
    • Coordination structure of active site in synthetic hemoprotein (albumin-heme) with dioxygen and carbon monoxide
    • Tsuchida, E., Nakagawa, A., and Komatsu, T. (2003) Coordination structure of active site in synthetic hemoprotein (albumin-heme) with dioxygen and carbon monoxide. Macromol. Symp. 195, 275-280.
    • (2003) Macromol. Symp. , vol.195 , pp. 275-280
    • Tsuchida, E.1    Nakagawa, A.2    Komatsu, T.3
  • 28
    • 0002192918 scopus 로고
    • Purification and physicochemical properties of recombinant human serum albumin
    • (Rival, C, Stoltz, J.-F., Eds.), John Libbey Eurotext, Montrouge
    • Sumi, A., Ohtani, W., Kobayashi, K., Ohmura, T., Yokoyama, K., Nishida, M., and Suyama, T. (1993) Purification and physicochemical properties of recombinant human serum albumin. Biotechnology of Blood Proteins (Rival, C, Stoltz, J.-F., Eds.) Vol. 227, pp 293-298, John Libbey Eurotext, Montrouge.
    • (1993) Biotechnology of Blood Proteins , vol.227 , pp. 293-298
    • Sumi, A.1    Ohtani, W.2    Kobayashi, K.3    Ohmura, T.4    Yokoyama, K.5    Nishida, M.6    Suyama, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.