1. Moosavi-Movahedi, A.A. (1994) Interaction of Asperjillus niger catalase with sodium n-dodecyl sulphate. Pure Appl. Chem. 66, 71-75
  2. Jones, M.N. (1977) A microcalorimetric study of the interaction between trypsin and sodium n-dodecyl sulphate. Biochim. Biophys. Acta 491, 121-128 [Medline]
  3. Moosavi-Movahedi, A.A., Naderi, G.A., and Farzami, B. (1994) The denaturation behaviour of calmodulin in sodium n-dodecyl, dodecyl trimethyl ammonium bromide, guanidine hydrochloride and urea. Thermochim. Acta 239, 61-71
  4. Hilak, M.C., Harmsen, B.J.M., Braam, W.G.M., Joordens, J.M., and Vanos, G.A.J. (1974) Conformational studies on large fragments of bovine serum albumin in relation to the structure of the molecule. Int. J. Pept. Protein Res. 6, 95-101 [Medline]
  5. Nazari, K., Saboury, A.A., and Moosavi-Movahedi, A.A. (1997) Enthalpy investigation for elucidation of the transition concentration for the interaction of horseradish peroxidase with surfactants. Thermochim. Acta 302, 131-135
  6. Saboury, A.A., Bordbar, A.K., and Moosavi-Movahedi, A.A. (1996) The enthalpy of unfolding for jack bean urease with interaction of 28, 1077-1082
  7. Jones, O.T., Earnest, J.P., and McNamee, M.G. (1987) Solubilization and reconstitution of membrane proteins in Biological Membranes: a Practical Approach (Findley, J.B.C. and Evance, W.H., eds.) pp. 139-177, IRL Press, Oxford
  8. Henselman, R.A. and Cusanovich, M.A. (1974) The characterization of sodium cholate solubilized rhodopsin. Biochemistry 13, 5199-5203 [Medline]
  9. Zorn, M. and Futterman, S. (1973) Extraction, regeneration, after bleaching, and ion-exchange chromatography of rhodopsin in Tween 80. Arch. Biochem. Biophys. 157, 91-99 [Medline]
  10. Osborne, H.B., Sardet, C., and Helenius, A. (1974) Bovine rhodopsin: characterization of the complex formed with Triton X-100. Eur. J. Biochem. 44, 383-390 [Medline]
  11. Markino, S., Reynolds, A.J., and Tanford, C. (1973) The binding of deoxycholate and Triton X-100 to proteins. J. Biol. Chem. 248, 4926-4932 [Medline]
  12. Stubbs, G.W., Smith, Jr.H.G., and Litman, B.J. (1976) Effect of alterations in the amphipathic microenvironment on the confomational stability of bovine opsin. Mechanism of solubilization of disk membranes by the nonionic detergent, octyl glucoside. Biochim. Biophys. Acta 425, 46-56
  13. Newman, M.J. and Wilson, T.H. (1980) Solubilization and reconstitution of the lactose transport system from Escherichia coli. J. Biol. Chem. 255, 10583-10586 [Medline]
  14. Markovic-Housley, Z. and Garavito, R.M. (1986) Effect of temperature and low pH on structure and stability of matrix porin in micellar detergent solutions. Biochim. Biophys. Acta 869, 158-170 [Medline]
  15. Baron, C. and Thompson, T.E. (1975) Solubilization of bacterial membrane proteins using alkyl glucosides and dioctanoyl phosphatidylcholine. Biochim. Biophys. Acta 382, 276-285 [Medline]
  16. Cordoba, J., Reboiras, M.D., and Jones, M.N. (1988) Interaction of n-octyl-b-D-glucopyranoside with globular proteins in aqueous solution. Int. J. Biol. Macromol. 10, 270-276
  17. Racker, E. (1983) Resolution and reconstitution of biological pathways from 1919 to 1984. Fed. Proc. 42, 2899-2909 [Medline]
  18. Cassman, M. and Schachman, H.K. (1971) Sedimentation equilibrium studies on glutamate dehydrogenase. Biochemistry 10, 1015-1024 [Medline]
  19. Moon, K., Piszkiewicz, D., and Smith, E. (1972) Glutamate dehydrogenase amino-acid sequence of the bovine enzyme and comparison with that from chicken liver. Pro. Natl. Acad. Sci. USA 69, 1380-1383
  20. Fisher, H.F. (1985) L-Glutamate dehydrogenase from bovine liver. Methods Enzymol. 113, 16-27 [Medline]
  21. Pour-Rahimi, F. and Nemat-Gorgani, M. (1987) Reversible association of ox liver glutamate dehydrogenase with the inner mitochondrial membrane. Int. J. Biochem. 19, 53-61 [Medline]
  22. Nemat-Gorgani, M. and Dodd, G.H. (1977) The interaction of phospholipid membranes and detergents with glutamate dehydrogenase: kinetic studies. Eur. J. Biochem. 74, 129-137
  23. Dodd, G.H. (1973) The interaction of glutamate dehydrogenase and malate dehydrogenase with phospholipid membranes. Eur. J. Biochem. 33, 418-427 [Medline]
  24. Julliard, J.H. and Gautheron, D.C. (1972) Regulatory effects of mitochondrial lipids on glutamate dehydrogenase (NAD(P)). FEBS Lett. 25, 343-345
  25. Godinot, C. (1973) Nature and possible functions of association between glutamate dehydrogenase and cardiolipin. Biochemistry 12, 4029-4043 [Medline]
  26. Nemat-Gorgani, M. and Dodd, G.H. (1977) The interaction of phospholipid membranes and detergents with glutamate dehydrogenase: fluorescence and stopped-flow studies. Eur. J. Biochem. 74, 139-147 [Medline]
  27. Olson, J.A. and Anfinsen, C.B. (1952) The crystallization and characterization of L-glutamic acid dehydrogenase. J. Biol. Chem. 197, 67-79
  28. Chalabi, P., Maniscalco, S., Cohn, L.E., and Fisher, H.F. (1987) The effects of an acetate-sensitive anion binding site on NADPH binding in glutamate dehydrogenase. Biochim. Biophys. Acta 913, 103-110 [Medline]
  29. Spiro, R.G. (1966) Analysis of sugars found in glycoproteins. Methods Enzymol. 8, 3-26
  30. Schippers, P.H. and Dekkers, H.P.J.M. (1981) Direct determination of absolute circular dichroism data and calibration of commercial instrument. Anal. Chem. 53, 778-788
  31. Protasevich, I., Ranjbar, B., Lobachov, V., Makarov, A., Gilli, R., Briand, C., Lafitte, D., and Haiech, J. (1997) Conformation and thermal denaturation of apocalmodulin: role of electrostatic mutations. Biochemistry 36, 2017-2024 [Medline]
  32. Jones, M.N., Paz-Andrade, M., and Skinner, H.A. (1978) Enthalpy of interaction between some cationic polypeptides and n-alkyl sulphates in aqueous solution. J. Chem. Soc. Faraday Trans. 1 74, 2923-2929
  33. Tipping, E., Jones, M.N., and Skinner, H.A. (1974) Enthalpy of interaction between some globular proteins and sodium n-dodecyl sulphate in aqueous solution. J. Chem. Soc. Faraday Trans. 1 70, 1306-1315
  34. Wyman, J. (1965) The binding potential, a neglected linkage concept. J. Mol. Biol. 11, 631-644
  35. Jones, M.N. and Manley, P. (1981) Relationship between proton and surfactant binding to lysozyme in aqueous solution. J. Chem. Soc. Faraday Trans. 1 77, 827-835
  36. Prieto, G., del Rio, J.M., Paz Andrade, M.I., Sarmiento, F., and Jones, M.N. (1993) Interaction between sodium n-undecyl sulfate and insulin. Int. J. Biol. Macromol. 15, 343-345 [Medline]
  37. Bordbar, A.K. and Moosavi-Movahedi, A.A. (1996) Binding data analysis of the interaction of bovine hemoglobin with dodecyltrimethylammonium bromide. Bull. Chem. Soc. Jpn. 69, 2231-2234
  38. Bordbar, A.K., Moosavi-Movahedi, A.A., and Saboury, A.A. (1996) Comparative thermodynamic stability of bovine and pigeon haemoglobins by interaction with sodium n-dodecyl sulfate. Thermochim. Acta 284, 343-349
  39. Piszkiewicz, D., London, M., and Smith, E.L. (1973) Sequence of bovine liver glutamate dehydrogenase. J. Biol. Chem. 248, 3067-3081 [Medline]
  40. Kelly, S.M. and Price, N.C. (1997) Application of circular dichroism to studies of protein folding and unfolding. Biochim. Biophys. Acta 1338, 161-185 [Medline]
  41. Sears, D.W. and Beyckok, S. (1973) Physical Principles and Techniques of Protein Chemistry (Leach, S.J., ed.) Part C, pp. 445-593, Academic Press, New York
  42. Dolgikh, D.A., Gilmanshin, R.I., Brazhnicov, E.V., Bychkova, V.E., Semisotnov, G.V., Venyaminov, S.Yu., and Ptitsyn, O.B. (1981) a-Lactalbumin: compact state with fluctuating tertiary structure. FEBS Lett. 136, 311-315 [Medline]
  43. Ptitsyn, O.B. (1992) The molten globule state in Protein Folding (Creighton, T.E., ed.) pp. 243-300, W.H. Freeman and Company, New York
  44. Goto, Y. and Fink, A.L. (1990) Phase diagram for acidic conformational states of apomyoglobin. J. Mol. Biol. 214, 803-805 [Medline]
  45. Goto, Y., Hagihara, Y., Hamada, D., Hoshino, M., and Nishii, I. (1993) Acid-induced unfolding and refolding transitions of cytochrome c. A three state mechanism in H2O and D2O. Biochemistry 32, 11878-11885 [Medline]
  46. Bychova, V.E., Pain, R.H., and Ptitsyn, O.B. (1988) The molten globule state is involved in the translocation of protein across membranes. FEBS Lett. 238, 231-234 [Medline]
  47. Ptitsyn, O.B. (1995) Molten globule and protein folding. Adv. Protein Chem. 47, 83-229 [Medline]
  48. Stryer, L. (1965) The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13, 482-495 [Medline]
  49. Semisotnov, G.V., Rodionova, N.A., Razgulyaev, O.I., Uversky, V.N., Gripas, A.F., and Gilmanshin, R.I. (1991) Study of the molten globule intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 31, 119-128 [Medline]
  50. Semisotnov, G.V., Rodinova, N.A., Kutyshenko, V.P., Ebert, B., Blank, J., and Ptitsyn, O.B. (1987) Sequential mechanism of refolding of carbonic anhydrase. FEBS Lett. 224, 9-13 [Medline]
  51. Frieden, C. (1959) Glutamate dehydrogenase. J. Biol. Chem. 234, 815-825
  52. Delabar, J.M., Martin, S.R., and Bayley, P.M. (1982) The binding of NADH and NADPH to bovine-liver glutamate dehydrogenase; spectroscopic characterisation. Eur. J. Biochem. 127, 367-374 [Medline]
  53. Koberstein, R. and Sund, H. (1973) Studies of glutamate dehydrogenase. Eur. J. Biochem. 36, 545-552 [Medline]
  54. Ghobadi, S., Nemat-Gorgani, M., Golabi, S.M., Zare, H.R., and Moosavi-Movahedi, A.A. (2000) Nickel-induced substrate inhibition of bovine liver glutamate dehydrogenase. J. Enz. Inhibition 15, 497-508