Effect of physiological concentration of urea on the conformation of human serum albumin

Journal of Biochemistry

Volumn 141, Issue 2, 2007, Pages 261-268

  Gull, Nuzhat ^a   Sen, Priyankar ^a   Kabir ud Din, ^a   Khan, Rizwan Hasan ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

ANS binding and human serum albumin; Circular dichroism; Intrinsic fluorescence; Monomethyl urea; Urea

Indexed keywords

HUMAN SERUM ALBUMIN; MONOMETHYLUREA; UNCLASSIFIED DRUG; UREA;

ALPHA HELIX; ARTICLE; DIELECTRIC CONSTANT; HYDROPHOBICITY; PH; PROTEIN CONFORMATION; PROTEIN STRUCTURE; SPECTROFLUOROMETRY;

ANILINO NAPHTHALENESULFONATES; CIRCULAR DICHROISM; FLUORESCENCE; HUMANS; METHYLUREA COMPOUNDS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SERUM ALBUMIN; SOLVENTS; UREA;

EID: 34248640314     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvm027     Document Type: Article

References (67)

1. Qui, L. and Hagen, S.J. (2004) A limiting speed for protein folding at low solvent viseoeity. J. Am. Chem. Soc. 126, 3398-3399
2. He, X.M. and Carter, D.C. (1992) Atomic structure and chemistry of human serum albumin. Nature 358, 209-215
3. Nishimura, C., Dyson, H.J., and Wright, P.E. (2005) Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench experiments. Proc. Natl Acad. Sci. 102, 4765-4770
4. Ahmad, B., Ahmad, M.Z., Haq, S.K., and Khan, R.H. (2005) Guanidine hydrochloride denaturation of human serum albumin originates by local unfolding of some stable loops in domain III. Biochim. Biophys. Acta 1750, 93-102
5. Ahmad, B. and Ankita Khan, R.H. (2005) Urea induced unfolding of F isomer of human serum albumin: A case study using multiple probes. Arch. Biochem. Biophys. 437, 159-167
6. Itri, R., Caetano, W., Barbosa, L.R.S., and Baptista, M.S. (2004) Effect of urea on bovine serum albumin in aqueous and reverse micelle environments investigated by small angle x-ray scattering, flourescence and circular dichroism. Braz. J. Phys. 341, 58-64
7. Muzammil, S., Kumar, Y., and Tayyab, S. (2000) Anion-induced refolding of human serum albumin under low pH conditions. Proteins Struct. Funct. Conet. 40, 29-38
8. Enea, O. and Jollcoeur, C. (1982) Heat capacities and volumes of several oligopeptides in urea-water mixtures at 25.degree.C Some implications for protein unfolding. J. Phys. Chem. 86, 3870-3881
9. Liepnish, E. and Otting, G. (1994) Specificity of urea binding to proteins. J. Am. Chem. Soc. 116, 9670-9674
10. Ruiz, C.C. (1999) Micelle formation and microenvironmental properties of sodium dodecyl sulfate in Aqueous Solutions. Colloids Surf. A 147, 349-357
11. Constantino, L., D' Errico, G., Roscigno, P., and Vitagliano, V. (2000) Effect of urea and alkylureas on micelle formation by a nonionic surfactant with short hydrophobic tail at 25 C. J. Phys. Chem. B 104, 7326-7333
12. Nozaki, Y. and Tanford, C. (1963) The Solubility of amino acids and related compounds in aqueous urea solutions. J. Biol. Chem. 238, 4074-4081
13. Kauzmann, W. (1954) Denaturants of proteins and enzymes in The Mechanism of Enzyme Action (Mcelory, W.D. and Glass, B., eds) pp. 70-110, Johns Hopkins Press, Baltimore
14. Tanford, C. (1958) The configuration of globular proteins in Symposium on Protein Structure (Neuberger, A., ed.) pp. 35-65, Mathuen and Company, London
15. Klotz, I.M. (1958) Protein hydration and behaviour. Science 128, 815-822
16. Kauzmann, W. (1959) Advances in Protein Chemistry (Anfinson, Jr., Anson, M.L., Bailey, K., and Edsall, J.T., eds) Vol. 14, pp. 1, Academic Press, Inc., New York
17. Tanford, C. (1962) Contribution of hydrophobic interactions to the stability of the globular conformation of proteins. J. Am. Chem. Soc. 84, 4240-4247
18. Tanford, C. and De, P.K. (1961) The unfolding of β-lactoglobulin at pH 3 by urea, formamide and other organic substances. J. Biol. Chem. 236, 1711-1715
19. Hotz, I.M. and Franzen, J.S. (1962) The unfolding of β-lactoglobulin at pH 3 by urea, formamide and other organic substances. J. Am. Chem. Soc. 84, 3461-3466
20. Manabe, M., Koda, M., and Shirahama, K.J. (1980) The effect of 1-alkanols on ionization of Sodiumdodecylsulfate. Colloid Interface Sci. 77, 189-194
21. Bonner, O.D., Dednarek, J.M., and Arisman, R.K. (1977) Heat capacities of ureas and water in water and dimethyl-formamide. J. Am. Chem. Soc. 99, 2898-2902
22. Herskovics, T.T. and Kelly, T.M. (1973) Viscosity studies of aqueous solutions of alcohols, ureas, and amides. J. Phys. Chem. 77, 381-388
23. Frank, H.S. and Evans, M.W. (1945) Free volume and entropy in condensed systems. J. Chem. Phys. 13, 507-532
24. Tanford, C. (1962) Contribution of hydrophobic interactions to the stability of the globular conformation of proteins. J. Am. Chem. Soc. 84, 4240-4247
25. Courtney, E.S., Cap, M.W., and Record, J.M. (2001) Vapour pressure osmometry studies of Osmolyte-Protein Interaction: implication for the action of Osmoprotectants in vivo and for the interpretation of "osmotic stress" experiments in vitro. Science 10, 2485-2485
26. Chandler, D. (2002) Two faces of water. Nature 417, 491
27. Kumar, S., Parveen, N., and Kabir-ud-Din, (2004) Effect of urea addition on micellization and the related phenomena. J. Phys. Chem. B 108, 9588
28. Gull, N., Kumar, S., Ahmed, B., Khan, R.H., and Kabir-ud-Din., (2006) Influence of urea additives on micellar morphology/protein conformation. Colloids Surf. B. 51, 10-15
29. Peters, T.J. (1985) Serum albumins in Advances in Protein Chemistry. Vol. 37, pp. 161-245, Academic press, New York
30. Lindup, W.E. (1987) Plasma protein binding of drugs-some basic and chemical aspects. Prog. Drug. Metab. 10, 141-185
31. Brown, J.R. (1977) Serum albumin: amino acid sequence in Albumin Structure, Function and Uses (Rosenoer, V.M. and Rothschild, M.A., eds) pp. 27-51, Pergamon, Oxford
32. Carter, D., Chang, B., Ho, J.X., and Keeling Krishnaswamy, Z. (1994) Preliminary crystallographic studies of four crystal forms of serum albumins. Eur. J Biochem. 226, 1049-1052
33. Peters, T.J., (1996) (Metabolism: Albumin in the body) All About Albumin Biochemistry, Genetics, And Medical Applications (Peters, T., ed.), Academic Press Limited, New York
34. Carter, D.C. and Ho, J.X. (1994) Structure of serum albumin Adv. Protein Chem. 45, 153-203
35. Ahmad, B., Kamal, M.J., and Khan, R.H. (2004) AlkaliInduced Conformational Transition in Different Domains of Bovine Serum Albumin. Pro. And Pep. Lett. 4, 307-315
36. Wallevik, K. (1973) Reversible denaturation of human serum albumin by pH, temperature, and Guanidine hydrochloride followed by optical rotation. J. Biol. Chem. 245, 2650
37. Lowry, O.H., Rosenbrough., , Farr, A.L., and Randall, R.J. (1951) Protein measurement with the Folin-Phenol reagent. J. Biol. Chem. 193, 265-275
38. Adrade, M.A., Chacon, P., Merelo, J.J., and Moran, F. (1993) Evaluation of secondary structure of proteins from UV Circular dichroism using an unsupervised network. Protein Eng. 6, 383-390
39. Carbin, J., Methlot, N., Wang, H.H., Baenziger, J.E., and Blanton, P. (1998) Secondary structure analysis of individual transmembrane segments of the nicotinic acetylcholine receptor by circular dichroism and fourier transform infrared spectroscopy. J. Biol. Chem. 273, 771-777
40. Chen, R.F. (1974) Fluorescence stopped-flow study of relaxation processes in the binding of billirubin to serum albumins. Arch. Biochem. Biophys. 160, 106-112
41. Liu, R., Yang, J., Ha, C.E., Bhagavan, N.V., and Eckenhoff, R.G. (2005) Truncated human serum albumin retainsgeneral anaesthetic binding activity. Biochem. J. 388, 39-45
42. Dockal, M., Carter, D.C., and Ruker, F. (2000) Conformational transitions of the three recombinant domains of human serum albumins depending on pH. J. Biol. Chem. 275, 3042-3050
43. Provencher, S.W. and Glockner, J. (1981) Estimation of globular secondary structure from circular dichroism. Biochemistry 20, 33-37
44. Dryden, D. and Weir, M.P. (1991) Evidence of an acid-induced molten-globule state in interleukin-2, a fluorescence and circular dichroism study. Biochim. Biophys. Acta 1078, 94-100
45. Lee, J.H. and Hirose, M (1992) Effects of disulphide reduction on the emulsifying properties of bovine serum albumin. J. Biol. Chem. 267, 14733-14752
46. Chen, Y. and Barkley, M.D. (1998) Towards understanding tryptophan fluorescence in proteins. Biochemistry 37, 9976-9982
47. Pace, C.N., Vajdos, F., Fee, L., Grimsley, W., and Gray, T. (1995) How to measure and predict the Molar Adsorption Coefficient of a protein. Protein Sci. 4, 2411-2423
48. Ghisla, S., Massey., V., Lhoste, J.M., and Mayhew, S. (1974) Fluorescence and optical characteristics of reduced flavins and flavoproteins. Biochemistry 13, 589-597
49. Tanford, C. (1973) The Hydrophobic Effect: formation of micelles and biological membranes. Wiley-Interscience publication. Chapter 14, pp. 123, New York
50. Stryer, L. (1965) The Interaction of a naphthalene dye with apomyoglobin and apohemoglobin, a fluorescent probe for nonpolar sites. J. Mol. Biol. 13, 482-495
51. Matulis, D. and Lovrien, R. (1998) 1-anilino-8-naphthalene-sulphonate anion-protein binding depends primarily on ion pair formation. Biophys. J. 74, 422-429
52. Slavik, J. (1982) Anilinonaphthalene sulphonate as a probe of membrane composition and function. Biochem. Biophys. Acta 694, 1-25
53. Daniel, E. and Weber, G. (1966) Cooperative effects in binding by bovine serum albumin: The binding of 1-anilino-8-naphthalenesulphonate, fluorimetric titrations. Biochemistry 5, 1893-1900
54. Denny, M.W. (1993) Air and Water: The Biology and Physics of life's media, Princeton university, Princeton
55. Baptista, M.S. and Trans, C.D. (1995) Structural investigation of the effects of nonelectrolytse and surfactantson water by spectroscopy. J. Phys. Chem. 99, 12952-12961
56. Bhanumathi, R. and Vijayalakshmi, S.K. (1986) Proton NMR chemical shifts of solvent water in aqueous solutions of monosubstituted ammonium compounds. J. Phys. Chem. 90, 4666-4669
57. Abu-Hamidiyyah, M. and Al-Mansour, L. (1979) Effect of butylurea on the critical micelle concentration of sodium lauryl sulfate in water at different temperatures. J. Phys. Chem. 83, 2236-2243
58. Wallqvist, A., Covell, D.G., and Thirumalai, D. (1998) Hydrophobic interactions in aqueous urea solutions with implications for the mechanism of protein denaturation. J. Am. Chem. Soc. 120, 427
59. Bhuyan, A.K. (2002) Protein Stabilization by Urea and Guanidine Hydrochloride. Biochemistry 41, 13386
60. Venkatesan, V.K. and Suryanarayanna, C.V. (1956) Conductance and other physical properties of aqueous solutions. J. Phys. Chem. 60, 775-776
61. Kumar, A.R., Hegde, S.S., Ganesh, K.N., and Khan, M.I. (2003) Structural changes enhance the activity of chainea xylanase in low urea concentrations. Biochim. Biophys. Acta 1645, 164-171
62. Schick, M.J. (1964) Effect of electrolyte and urea on micelle formation. J. Phys. Chem. 68, 3585-3587
63. Carvalho, B.L., Briganti, G., and Chen, S.H. (1989) Lowering of the miscibility gap in the dioctanoylphosphatidylcholine-water system by addition of urea. J. Phys. Chem. 93, 4282-4286
64. Goldammer, E.V. and Hertz, H.G. (1970) Molecular motion and structure of aqueous mixtures with nonelectrolytes as studied by nuclear magnetic relaxation methods. J. Phys. Chem. 74, 3734-3755
65. Ben-Naim, A. (1980) Hydrophobic Interactions. pp. 81-82 Plenum Press, New York
66. Arakawa, T. and Goldette, D. (1985) The mechanism of helical transition of proteins by organic solvents. Arch. Biochim. Biophys. 240, 21-32
67. Apetri, A.C. and Surewicz, W.K. (2003) Atypical effect of salts on the thermodynamic stability of human prion protein. J. Biol. Chem. 278, 22187-22192