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Volumn 62, Issue 6, 1996, Pages 613-620

The effect of concentration on the structure of α-crystallin

Author keywords

conformation; micelle; quaternary structure; tertiary structure; crystallin

Indexed keywords

ALPHA CRYSTALLIN; BOVINE SERUM ALBUMIN; DODECYL SULFATE SODIUM; PROTEIN SUBUNIT; TRYPTOPHAN;

EID: 0030008361     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.1996.0072     Document Type: Article
Times cited : (10)

References (35)
  • 1
    • 0023667137 scopus 로고
    • A possible structure for α-crystallin
    • Augusteyn, R. C. and Koretz, J. F. (1987). A possible structure for α-crystallin. FEBS Lett. 222, 1-5.
    • (1987) FEBS Lett. , vol.222 , pp. 1-5
    • Augusteyn, R.C.1    Koretz, J.F.2
  • 2
    • 0026563561 scopus 로고
    • The effects of isolation buffers on the properties of α-crystallin
    • Augusteyn, R. C., Parkhill, E. M. and Stevens, A. (1992). The effects of isolation buffers on the properties of α-crystallin. Exp. Eye Res. 54, 219-28.
    • (1992) Exp. Eye Res. , vol.54 , pp. 219-228
    • Augusteyn, R.C.1    Parkhill, E.M.2    Stevens, A.3
  • 3
    • 0023858779 scopus 로고
    • Quenching of tryptophan fluorescence in bovine lens proteins by acrylamide and iodine
    • Augusteyn, R. C., Putilina, T. and Seifert, R. (1988). Quenching of tryptophan fluorescence in bovine lens proteins by acrylamide and iodine. Curr. Eye Res. 7, 237-45.
    • (1988) Curr. Eye Res. , vol.7 , pp. 237-245
    • Augusteyn, R.C.1    Putilina, T.2    Seifert, R.3
  • 4
    • 0018574180 scopus 로고
    • A model for the architecture of α-crystallin
    • Bindels, J. G., Siezen, R. J. and Hoenders, H. J. (1979). A model for the architecture of α-crystallin. Ophthal. Res. 11, 441-52.
    • (1979) Ophthal. Res. , vol.11 , pp. 441-452
    • Bindels, J.G.1    Siezen, R.J.2    Hoenders, H.J.3
  • 5
    • 0018192767 scopus 로고
    • Fluorescence spectra of tryptophan residues in human and bovine lens proteins
    • Borkman, R. F. and Lerman, S. (1978). Fluorescence spectra of tryptophan residues in human and bovine lens proteins. Exp. Eye Res. 26, 705-13.
    • (1978) Exp. Eye Res. , vol.26 , pp. 705-713
    • Borkman, R.F.1    Lerman, S.2
  • 7
    • 0025787736 scopus 로고
    • Micellar subunit assembly in three-layer model of oligomeric α-crystallin
    • Chakrabarti, B., Walsh, M. T. and Sen, A. C. (1991). Micellar subunit assembly in three-layer model of oligomeric α-crystallin. J. Biol. Chem. 266, 20079-84.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20079-20084
    • Chakrabarti, B.1    Walsh, M.T.2    Sen, A.C.3
  • 8
    • 0026534772 scopus 로고
    • Hypertonic stress induces αB-crystallin expression
    • Dasgupta, S., Hohman, T. C. and Carper, D. (1992). Hypertonic stress induces αB-crystallin expression. Exp. Eye Res. 54, 461-70.
    • (1992) Exp. Eye Res. , vol.54 , pp. 461-470
    • Dasgupta, S.1    Hohman, T.C.2    Carper, D.3
  • 9
    • 0020678719 scopus 로고
    • Short range order of crystallin proteins accounts for eye lens transparency
    • Delaye, M. and Tardieu, A. (1983). Short range order of crystallin proteins accounts for eye lens transparency. Nature 302, 415-17.
    • (1983) Nature , vol.302 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 11
    • 0343841475 scopus 로고
    • The effect of excess salt on minima observed in γ/LOG C curves for surface active agents
    • Harrold, S. P. (1959). The effect of excess salt on minima observed in γ/LOG C curves for surface active agents. J. Phys. Chem. 63, 317.
    • (1959) J. Phys. Chem. , vol.63 , pp. 317
    • Harrold, S.P.1
  • 12
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz, J. (1992). Alpha-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci., USA 89, 10449-53.
    • (1992) Proc. Natl. Acad. Sci., USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 13
    • 0027342592 scopus 로고
    • The function of alpha-crystallin
    • Horwitz, J. (1993). The function of alpha-crystallin. Invest. Ophthalmol. Vis. Sci. 34, 10-19.
    • (1993) Invest. Ophthalmol. Vis. Sci. , vol.34 , pp. 10-19
    • Horwitz, J.1
  • 14
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin
    • Ingolia, T. D. and Craig, E. A. (1982). Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin. Proc. Natl. Acad. Sci., USA 79, 2360-4.
    • (1982) Proc. Natl. Acad. Sci., USA , vol.79 , pp. 2360-2364
    • Ingolia, T.D.1    Craig, E.A.2
  • 15
    • 0024521440 scopus 로고
    • αB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain
    • Iwaki, T., Kume-Iwaki, A., Liem., R. K. H. and Goldman, J. E. (1989). αB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 57, 71-8.
    • (1989) Cell , vol.57 , pp. 71-78
    • Iwaki, T.1    Kume-Iwaki, A.2    Liem, R.K.H.3    Goldman, J.E.4
  • 16
    • 0028180509 scopus 로고
    • α-crystallin/small heat shock protein has autokinase activity
    • Kantorow, M. and Piatigorsky, J. (1994). α-crystallin/small heat shock protein has autokinase activity. Proc. Natl. Acad. Sci., USA 91, 3112-16.
    • (1994) Proc. Natl. Acad. Sci., USA , vol.91 , pp. 3112-3116
    • Kantorow, M.1    Piatigorsky, J.2
  • 17
    • 84981611610 scopus 로고
    • The fluorescence of native, denatured, and reduced denatured protein
    • Kronan, M. J. and Holmes, L. G. (1971). The fluorescence of native, denatured, and reduced denatured protein. Photochem. Photobiol. 14, 113-14.
    • (1971) Photochem. Photobiol. , vol.14 , pp. 113-114
    • Kronan, M.J.1    Holmes, L.G.2
  • 19
    • 0025073458 scopus 로고
    • Dementia with β-amyloid deposition. Involvement of αB-crystallin supports two main diseases
    • Lowe, J., Landon, M., Pike, I., Spendlove, I., McDermott, H. and Mayer, R. J. (1990). Dementia with β-amyloid deposition. Involvement of αB-crystallin supports two main diseases. Lancet 336, 515-16.
    • (1990) Lancet , vol.336 , pp. 515-516
    • Lowe, J.1    Landon, M.2    Pike, I.3    Spendlove, I.4    McDermott, H.5    Mayer, R.J.6
  • 21
    • 0019305133 scopus 로고
    • Thermodynamic basis for the abnormal solubility of monoclonal cryoimmunoglobulins
    • Middaugh, C. R. and Lawson, E. Q. (1980). Thermodynamic basis for the abnormal solubility of monoclonal cryoimmunoglobulins. J. Biol. Chem. 255, 6532-4.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6532-6534
    • Middaugh, C.R.1    Lawson, E.Q.2
  • 22
    • 0002150958 scopus 로고
    • Minima in surface tension - Concentration curves of solutions of Na alcohol sulfates
    • Miles, G. D. and Shedlovsky, L. (1944). Minima in surface tension - concentration curves of solutions of Na alcohol sulfates. J. Phys. Chem. 48, 57-62.
    • (1944) J. Phys. Chem. , vol.48 , pp. 57-62
    • Miles, G.D.1    Shedlovsky, L.2
  • 23
    • 0026527490 scopus 로고
    • Characterization of the elastase inhibitor properties of α-crystallin and the water-insoluble fraction from bovine lens
    • Ortwerth, B. J. and Olesen, P. R. (1992). Characterization of the elastase inhibitor properties of α-crystallin and the water-insoluble fraction from bovine lens. Exp. Eye Res. 54, 103-11.
    • (1992) Exp. Eye Res. , vol.54 , pp. 103-111
    • Ortwerth, B.J.1    Olesen, P.R.2
  • 24
    • 0026472559 scopus 로고
    • Phylogeny of the α-crystallin-related heat-shock proteins
    • Plesofsky-Vig, N., Vig, J. and Bramble, R. (1992). Phylogeny of the α-crystallin-related heat-shock proteins. J. Mol. Evol. 35, 537-45.
    • (1992) J. Mol. Evol. , vol.35 , pp. 537-545
    • Plesofsky-Vig, N.1    Vig, J.2    Bramble, R.3
  • 25
    • 0002789106 scopus 로고
    • Some correlating principles of detergent action
    • Preston, W. C. (1948). Some correlating principles of detergent action. J. Phys. Colloid Chem. 52, 84-97.
    • (1948) J. Phys. Colloid Chem. , vol.52 , pp. 84-97
    • Preston, W.C.1
  • 26
    • 0026506411 scopus 로고
    • Biophysical characterization of α-crystallin aggregates; validation of the micelle hypothesis
    • Radlick, L. W. and Koretz, J. F. (1992). Biophysical characterization of α-crystallin aggregates; validation of the micelle hypothesis. Biochim. Biophys. Acta 1120, 193-200.
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 193-200
    • Radlick, L.W.1    Koretz, J.F.2
  • 27
    • 0026228560 scopus 로고
    • Structural properties of polydisperse biopolymer solutions: A light scattering study of bovine α-crystallin
    • Schurtenburger, P. and Augusteyn, R. C. (1991). Structural properties of polydisperse biopolymer solutions: a light scattering study of bovine α-crystallin. Biopolymers 31, 1229-40.
    • (1991) Biopolymers , vol.31 , pp. 1229-1240
    • Schurtenburger, P.1    Augusteyn, R.C.2
  • 28
    • 0018172119 scopus 로고
    • The quaternary structure of bovine α-crystallin. Size and charge microheterogeneity: More than 1000 different hybrids?
    • Siezen, R. J., Bindels, J. G. and Hoenders, H. J. (1978). The quaternary structure of bovine α-crystallin. Size and charge microheterogeneity: more than 1000 different hybrids? Eur. J. Biochem. 91, 387-96.
    • (1978) Eur. J. Biochem. , vol.91 , pp. 387-396
    • Siezen, R.J.1    Bindels, J.G.2    Hoenders, H.J.3
  • 29
    • 0027421178 scopus 로고
    • Acid-induced dissociation of α A-and αB-crystallin homopolymers
    • Stevens, A. and Augusteyn, R. C. (1993). Acid-induced dissociation of α A-and αB-crystallin homopolymers. Biophys. J. 65, 1648-55.
    • (1993) Biophys. J. , vol.65 , pp. 1648-1655
    • Stevens, A.1    Augusteyn, R.C.2
  • 30
    • 0023721503 scopus 로고
    • Eye lens proteins and transparency: From light transmission theory to solution X-ray structural analysis
    • Tardieu, A. and Delaye, M. (1988). Eye lens proteins and transparency: From light transmission theory to solution X-ray structural analysis. Ann. Rev. Biophys. Biochem. 17, 47-70.
    • (1988) Ann. Rev. Biophys. Biochem. , vol.17 , pp. 47-70
    • Tardieu, A.1    Delaye, M.2
  • 31
    • 0022887592 scopus 로고
    • Calf lens α-crystallin quaternary structure. A three layered tetrahedral model
    • Tardieu, A., Laporte, D., Licinio, P., Krop, B. and Delaye, M. (1986). Calf lens α-crystallin quaternary structure. A three layered tetrahedral model. J. Mol. Biol. 192, 711-24.
    • (1986) J. Mol. Biol. , vol.192 , pp. 711-724
    • Tardieu, A.1    Laporte, D.2    Licinio, P.3    Krop, B.4    Delaye, M.5
  • 33
    • 0025106497 scopus 로고
    • Hydrostatic pressure studies of native and synthetic thick filaments: In vitro myosin aggregates at pH 7.0 with and without C-protein
    • Tumminia, S. J., Kortez, J. F. and Landau, J. V. (1990). Hydrostatic pressure studies of native and synthetic thick filaments: in vitro myosin aggregates at pH 7.0 with and without C-protein. Biochim. Biophys. Acta 1040, 373-81.
    • (1990) Biochim. Biophys. Acta , vol.1040 , pp. 373-381
    • Tumminia, S.J.1    Kortez, J.F.2    Landau, J.V.3
  • 34
    • 9144248184 scopus 로고
    • The critical micelle concentration of sodium lauryl sulphate at 25°C
    • Williams, R. J., Phillips, J. N. and Mysels, K. J. (1955). The critical micelle concentration of sodium lauryl sulphate at 25°C. Trans. Faraday Soc. 51, 728-37.
    • (1955) Trans. Faraday Soc. , vol.51 , pp. 728-737
    • Williams, R.J.1    Phillips, J.N.2    Mysels, K.J.3
  • 35
    • 0027229257 scopus 로고
    • Possible tetramer-based quaternary structures for a-crystallin and small heat shock proteins
    • Wistow, G. (1993). Possible tetramer-based quaternary structures for a-crystallin and small heat shock proteins. Exp. Eye Res. 56, 729-32.
    • (1993) Exp. Eye Res. , vol.56 , pp. 729-732
    • Wistow, G.1


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