참고문헌
- Bhattacharya, A. A., Grüne, T. and Curry, S. (2000) Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. J. Mol. Biol. 303, 721-732. https://doi.org/10.1006/jmbi.2000.4158
- Bougie, I., Parent, A. and Bisaillon, M. (2004) Thermodynamics of ligand binding by the yeast mRNA-capping enzyme reveals different modes of binding. Biochem. J. 384, 411-420. https://doi.org/10.1042/BJ20041112
- Brown, J. R. (1977) Albumin structure, function and uses, Rosenoer, V. M., Oratz, M., Rothschild, M. A. (eds.), Pergamon Press, Oxford, UK.
- Carter, D. C. and Ho, J. X. (1994) Structure of serum albumin. Adv. Protein Chem. 45, 153-203. https://doi.org/10.1016/S0065-3233(08)60640-3
- Chen, Y. H., Yang, J. T. and Martinez, H. M. (1972) Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11, 4120-4131. https://doi.org/10.1021/bi00772a015
- Curry, S., Mandelkow, H., Brick, P. and Franks, N. (1998) Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nature Struct. Biol. 5, 827-835. https://doi.org/10.1038/1869
- Curry, S., Brick, P. and Franks, N. P. (1999) Fatty acid binding to human serum albumin: new insights from crystallographic studies. Biochim. Biophys. Acta 1441, 131-140. https://doi.org/10.1016/S1388-1981(99)00148-1
- Dill, K. A., Alonso, D. O. V. and Hutchinson, K. (1989) Thermal stabilities of globular proteins, Biochemistry 28, 5439-5449. https://doi.org/10.1021/bi00439a019
- Farruggia, B. and Pico, G. A. (1999) Thermodynamic features of the chemical and thermal denaturations of human serum albumin. Int. J. Biol. Macromol. 26, 317-323. https://doi.org/10.1016/S0141-8130(99)00054-9
- Farruggia, B., Rodriguez, F., Rigatuso, R., Fidelio, G. and Pico G. (2001) The participation of human serum albumin domains in chemical and thermal unfolding. J. Protein Chem. 20, 81-89. https://doi.org/10.1023/A:1011000317042
- Flora, K., Brennan, J. D., Baker, G. A., Doody, M. A and Bright, F. V. (1998) Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods. Biophys. J. 75, 1084-1096. https://doi.org/10.1016/S0006-3495(98)77598-8
- Galisteo, M., Mateo, P. and Sanchez-Ruiz, J. (1991) Kinetic study on the irreversible thermal denaturation of yeast phosphoglycerate kinase. Biochemistry 30, 2061-2066. https://doi.org/10.1021/bi00222a009
- Gelamo, E. L. and Tabak, M. (2000) Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants. Spectrochimica Acta A 56, 2255-2271. https://doi.org/10.1016/S1386-1425(00)00313-9
- Giancola, C., De Sena, C., Fessas, D., Graziano, G. and Barone, G. (1997) DSC studies on bovine serum albumin denaturation: Effects of ionic strength and SDS concentration. Int. J. Biol. Macromol. 20, 193-204. https://doi.org/10.1016/S0141-8130(97)01159-8
- He, X. M. and Carter, D. C. (1992) Atomic structure and chemistry of human serum albumin. Nature 358, 209-215. https://doi.org/10.1038/358209a0
-
Ikeguchi, M., Sugai, S., Fujino, M., Sugawara, T. and Kuwajima K. (1992) Contribution of the 6-120 disulfide bond of
$\alpha$ -lactalbumin to the stabilities of its native and molten globule states. Biochemistry 31, 12695-12700. - Kragh-Hansen, U. (1981) Molecular aspects of ligand binding to serum albumin. Pharmacol. Rev. 33, 17-53.
- Kragh-Hansen, U., Hellec, F., de Foresta, B., le Maire, M. and Moller J. V. (2001) Detergents as probes of hydrophobic binding cavities in serum albumin and other water-soluble proteins. Biophys. J. 80, 2898-2911. https://doi.org/10.1016/S0006-3495(01)76255-8
- Michnik, A. (2003) Thermal stability of bovine serum albumin: DSC study. J. Therm. Anal. Cal. 71, 509-519. https://doi.org/10.1023/A:1022851809481
- Moosavi-Movahedi, A. A., Naderi, G. A. and Farzami, B. (1994) The denaturation behaviour of calmodulin in sodium n-dodecyl sulphate, dodecyl trimethyl ammonium bromide, guanidine hydrochloride and urea. Thermochimica Acta 239, 61-71. https://doi.org/10.1016/0040-6031(94)87056-X
- Moosavi-Movahedi, A. A., Nazari, K. and Saboury, A. A. (1997) Denaturation of horseradish peroxidase with SDS and DTAB, Colloids Surf. B. Biointerfaces 9, 123-130. https://doi.org/10.1016/S0927-7765(97)00016-7
- Moosavi-Movahedi, A. A. (2005) Thermodynamics of protein denaturation by sodium dodecyl sulfate. J. Iran Chem. Soc. 2, 189-196. https://doi.org/10.1007/BF03245921
- Nielsen, A. D., Borch, K. and Westh, P. (2000) Thermochemistry of the specific binding of C12 surfactants to bovine serum albumin. Biochim. Biophys. Acta 1479, 321-331. https://doi.org/10.1016/S0167-4838(00)00012-1
- Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280. https://doi.org/10.1016/0076-6879(86)31045-0
- Pace, C. N. (1990) Conformational stability of globular proteins. Trends Biochem. Sci. 15, 14-17. https://doi.org/10.1016/0968-0004(90)90124-T
- Pico, G. A. (1997) Thermodynamic features of the thermal unfolding of human serum albumin. Int. J. Biol. Macromol. 20, 63-73. https://doi.org/10.1016/S0141-8130(96)01153-1
- Privalov, P. L. (1982) Stability of proteins. Proteins which do not present a single cooperative system. Adv. Protein Chem. 35, 1-104. https://doi.org/10.1016/S0065-3233(08)60468-4
- Privalov, P. L. (1996) Intermediate states in protein folding. J. Mol. Biol. 258, 707-725. https://doi.org/10.1006/jmbi.1996.0280
- Privalov, P. L. and Potekhin, S. A. (1986) Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol. 131, 4-51. https://doi.org/10.1016/0076-6879(86)31033-4
- Ptitsyn, O. B. (1994) Kinetic and equilibrium intermediates in protein folding. Protein Eng. 7, 593-596. https://doi.org/10.1093/protein/7.5.593
- Ptitsyn, O. B. (1995) Structures of folding intermediates. Curr. Opin. Struct. Biol. 5, 74-78. https://doi.org/10.1016/0959-440X(95)80011-O
- Redfield, C., Smith, R. A. G. and Dobson, C. M. (1994) Structural characterization of a highly-ordered 'molten globule' at low pH. Nat. Struct. Biol. 1, 23-29. https://doi.org/10.1038/nsb0194-23
- Rezaei-Tavirani, M., Moosavi-Movahedi, A. A., Saboury, A. A., Hakimelahi, G. H., Ranjbar, B. and Housaindokht M. R. (2002) Thermodynamic domain analysis of fresh and incubated human apotransferrin. Thermochimica Acta 383, 103-108. https://doi.org/10.1016/S0040-6031(01)00684-0
- Saboury, A. A., Hosseini-Kishani, F., Rezaei-Tawirani, M. and Ranjbar, B. (2003) Thermodynamic studies on the interaction of nickel with human serum albumin, Progress Biochem. Biophys. 30, 732-737.
- Santoro, M. and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27, 8063-8068. https://doi.org/10.1021/bi00421a014
- Shaklai, N., Garlick, R. L. and Bunn, H. F. (1984) Nonenzymatic glycosylation of human serum albumin alters its conformation and function. J. Biol. Chem. 259, 3812-3817.
- Sugio, S., Kashima, A.,. Mochizuki, S., Noda, M. and Kobayashi, K. (1999) Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 12, 439-446. https://doi.org/10.1093/protein/12.6.439
- Tanford, C. (1968) Protein denaturation. Adv. Protein Chem. 23, 121-282. https://doi.org/10.1016/S0065-3233(08)60401-5
- Wallevik, K. (1973) Reversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation. J. Biol. Chem. 248, 2650-2655.
- Wetlaufer, D. B. (1981) Folding of protein fragments, Adv. Protein Chem. 34, 61-92. https://doi.org/10.1016/S0065-3233(08)60518-5
- Wetzel, R., Becker, M., Behlke, J., Billwitz, H., Bohm, S., Ebert, B., Hamann, H., Krumbiegel, J. and Lassmann, G. (1980) Temperature behaviour of human serum albumin. Eur. J. Biochem. 104, 469-478. https://doi.org/10.1111/j.1432-1033.1980.tb04449.x
- Yamasaki, M., Yano, H. and Aoki, K. (1992) Differential scanning calorimetric studies on bovine serum albumin: III. Effect of sodium dodecyl sulphate. Int. J. Biol. Macromol. 14, 305-312. https://doi.org/10.1016/S0141-8130(05)80070-4
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