Pure Appl. Chem., 2010, Vol. 82, No. 1, pp. 39-55
http://dx.doi.org/10.1351/PAC-CON-09-01-18
Published online 2010-01-03
Immobilized metal-ion affinity systems for recovery and structure–function studies of proteins at molecular, supramolecular, and cellular levels
References
- 1. J. Nature 258, 598 (1975). ( , J. Carlson, I. Olsson, G. Belfrage. http://dx.doi.org/10.1038/258598a0)
- 2. M. A. Trends Biotechnol. 7, 71 (1989). ( . http://dx.doi.org/10.1016/0167-7799(89)90067-X)
- 3. R. J. Bioinorg. Chem. 4, 15 (1974). ( , H. E. Parker. http://dx.doi.org/10.1016/S0006-3061(00)80171-4)
- 4. J. Biochemistry 22, 1621 (1983). ( , B. Olin. http://dx.doi.org/10.1021/bi00276a015)
- 5. N. J. Chromatogr. 321, 93 (1985). ( , J. Porath. http://dx.doi.org/10.1016/S0021-9673(01)90426-1)
- 6. E. S. Proc. Natl. Acad. Sci. 86, 1811 (1989). ( , Y. J. Zhao, E. Sulkowski, J. Porath. http://dx.doi.org/10.1073/pnas.86.6.1811)
- 7. E. Trends Biotechnol. 3, 1 (1985). ( . http://dx.doi.org/10.1016/0167-7799(85)90068-X)
- 8. E. Bioessays 10, 170 (1989). ( . http://dx.doi.org/10.1002/bies.950100508)
- 9. E. J. Mol. Recognit. 9, 389 (1996). ( . http://dx.doi.org/10.1002/(SICI)1099-1352(199634/12)9:5/6<389::AID-JMR271>3.0.CO;2-3)
- 10. L. Anal. Biochem. 154, 250 (1986). ( , J. Porath. http://dx.doi.org/10.1016/0003-2697(86)90523-3)
- 11. M. A. Vijayalakshmi. Affinity Chromatography and Biological Recognition, p. 269, Academic Press, Orlando (1983).
- 12. F. H. Biotechnology 9, 150 (1991). .
- 13. Y. J. Chromatogr. 354, 511 (1986). ( , K. Nakamura, T. Hashimoto. http://dx.doi.org/10.1016/S0021-9673(01)87061-8)
- 14. L. Ann. N.Y. Acad. Sci. 413, 300 (1984). ( , M. A. Vijayalakshmi. http://dx.doi.org/10.1111/j.1749-6632.1983.tb47904.x)
- 15. D. A. P. Small, T. Atkinson, C. R. Lowe. Affinity Chromatography and Biological Recognition, p. 267, Academic Press, Orlando (1983).
- 16. M. B. J. Chromatogr., B 861, 64 (2008). ( , M. A. Vijayalakshmi, D. Todorova-Balvay, S. M. Bueno. http://dx.doi.org/10.1016/j.jchromb.2007.11.018)
- 17. G. LC–GC Eur. 11, 998 (1999). , R. Hahn, A. Jungbauer.
- 18. A. Anal. Chem. 72, 5693 (2000). ( , M. Barut, A. Strancar, D. Josic, T. Koloini. http://dx.doi.org/10.1021/ac000680o)
- 19. I. J. Chromatogr., A 1065, 59 (2005). ( , D. Nemec, A. Podgornik, T. Koloini. http://dx.doi.org/10.1016/j.chroma.2004.10.054)
- 20. M. B. Biotechnol. Prog. 21, 644 (2005). ( , F. M. Plieva, I. Y. Galaev, R. Hatti-Kaul, B. Mattiasson. http://dx.doi.org/10.1021/bp049615g)
- 21. E. J. Sep. Sci. 27, 921 (2004). ( , P. Nesterenko, B. Paull. http://dx.doi.org/10.1002/jssc.200401794)
- 22. G. E. Am. Biotechnol. Lab. 12, 36 (1994). .
- 23. E. Biotechnology 6, 1321 (1988). , W. Bannwarth, H. Dobeli, R. Gentz, D. Stuber.
- 24. J. W. Sep. Purif. Methods 20, 49 (1991). , R. L. Albright, N. H. Wang.
- 25. G. S. J. Biochem. Biophys. Methods 49, 313 (2001). ( . http://dx.doi.org/10.1016/S0165-022X(01)00206-8)
- 26. E. Makromol. Chem., Macromol. Symp. 17, 335 (1988). .
- 27. Z. El Rassi, Cs. Horvath. HPLC of Biological Macromolecules, p. 179, Marcel Dekker, New York (1990).
- 28. H. P. Biotechnol. Prog. 15, 928 (1999). ( , D. F. Bruley. http://dx.doi.org/10.1021/bp9901015)
- 29. E. J. Mol. Recognit. 9, 494 (1996). ( . http://dx.doi.org/10.1002/(SICI)1099-1352(199634/12)9:5/6<494::AID-JMR290>3.0.CO;2-F)
- 30. I. FEBS Lett. 209, 13 (1986). ( , S. Jalalpour, W. Southwick, P. Newsome, M. J. Browne, J. H. Robinson. http://dx.doi.org/10.1016/0014-5793(86)81075-4)
- 31. V. J. Immunol. Methods 181, 225 (1995). ( , J. J. Winzerling, M. A. Vijayalakshmi, J. Porath. http://dx.doi.org/10.1016/0022-1759(95)00006-V)
- 32. F. M. J. Biotechnol. 76, 157 (2000). ( , J. E. Vazquez, M. Ayala, L. Canaan-Haden, H. Bell, I. Rodriguez et al. http://dx.doi.org/10.1016/S0168-1656(99)00183-2)
- 33. N. A. J. Chromatogr., A 840, 195 (1999). ( , T. Kirschner, M. P. Smith, R. Hjorth, N. J. Titchener-Hooker. http://dx.doi.org/10.1016/S0021-9673(99)00188-0)
- 34. R. Arch. Biochem. Biophys. 365, 163 (1999). ( , S. Yelle, B. Nguyen-Quoc. http://dx.doi.org/10.1006/abbi.1999.1146)
- 35. Y. J. Eur. J. Biochem. 202, 1115 (1991). ( , E. Sulkowski, J. Porath. http://dx.doi.org/10.1111/j.1432-1033.1991.tb16478.x)
- 36. S. J. Chromatogr. 370, 315 (1996). ( , M. A. Vijayalakshmi. http://dx.doi.org/10.1016/S0021-9673(00)94702-2)
- 37. Y. Plant Physiol. Biochem. 41, 215 (2001). ( , G. Grenier-de March, V. Gomord, H. Adenier, L. Faye, M. A. Vijayalakshmi. http://dx.doi.org/10.1016/S0981-9428(03)00013-5)
- 38. R. R. Biotechnol. Prog. 9, 64 (1993). ( , M. M. Ataai. http://dx.doi.org/10.1021/bp00019a009)
- 39. M. C. J. Biol. Chem. 263, 7211 (1988). , T. C. Furman, T. D. Ingolia, C. Pidgeon.
- 40. C. Protein Expression Purif. 11, 53 (1997). , A. Breitholtz, H. Brink-Nilsson, T. Moks, M. Uhlen, B. Nilsson.
- 41. E. J. Chromatogr. 411, 177 (1987). ( , H. Doebeli, A. Schacher. http://dx.doi.org/10.1016/S0021-9673(00)93969-4)
- 42. A. Protein Eng. 7, 1277 (1994). ( . http://dx.doi.org/10.1093/protein/7.10.1277)
- 43. T. Appl. Microbiol. Biotechnol. 42, 73 (1994). ( , W. Wende, A. Pingound, U. Rinas. http://dx.doi.org/10.1007/BF00170227)
- 44. C. F. Protein Expr. Purif. 2, 95 (1991). ( , I. Suominen, C. E. Glatz. http://dx.doi.org/10.1016/1046-5928(91)90057-P)
- 45. M. J. Chromatogr., A 1109, 80 (2006). ( , M. Jarc, M. Banjac, V. Frankovic, K. Bencina, M. Merhar, V. Gaberc-Porekar, V. Menart, A. Strancar, A. Podgornik. http://dx.doi.org/10.1016/j.chroma.2005.08.057)
- 46. J. J. Chromatogr., B 745, 197 (2000). , A. Chakraborty, M. Geng, X. Zhang, A. Amini, M. Bina, F. Regnier.
- 47. L. J. Chromatogr., A 924, 359 (2001). ( , C. Sioma, F. Regnier. http://dx.doi.org/10.1016/S0021-9673(01)00900-1)
- 48. D. J. Chromatogr., A 1031, 87 (2004). , N. Penner, B. Slentz, H. Inerowicz, M. Rybalko, F. Regnier.
- 49. B. J. Mol. Recognit. 11, 211 (1998). ( , A. Kumar, I. Y. Galaev. http://dx.doi.org/10.1002/(SICI)1099-1352(199812)11:1/6<211::AID-JMR425>3.0.CO;2-Y)
- 50. A. J. Chromatogr. 644, 25 (1993). ( , G. Birkenmeier. http://dx.doi.org/10.1016/0021-9673(93)80116-P)
- 51. H. G. Biochim Biophys. Acta 1074, 69 (1991). , G. Birkenmeier, A. Otto, A. Kopperschlager, M. A. Vijayalakshmi.
- 52. E. J. Chromatogr., B 680, 189 (1996). , J. C. Capiod, C. Dessaint, L. Prin, M. A. Vijayalakshmi.
- 53. H. J. Chromatogr. 597, 357 (1992). ( , E. Nanak, N. Abdul, G. Birkenmeir, M. A. Vijayalakshmi. http://dx.doi.org/10.1016/0021-9673(92)80132-E)
- 54. K. Anal. Biochem. 234, 149 (1996). ( , F. Roy, M. A. Vijayalakshmi. http://dx.doi.org/10.1006/abio.1996.0066)
- 55. H. Science 293, 2101 (2001). ( , M. Bilgin, R. Bangham, D. Hall, A. Casamayor, P. Bertone, N. Lan, R. Jansen, S. Bidlingmaier, T. Houfek, T. Mitchell, P. Miller, R. A. Dean, M. Gerstein, M. Snyder. http://dx.doi.org/10.1126/science.1062191)
- 56. H. Proc. Natl. Acad. Sci. USA 96, 5634 (1999). ( , E. Wilson-Kubalek, R. A. Milligan, L. Teyton. http://dx.doi.org/10.1073/pnas.96.10.5634)
- 57. P. P. Biochemistry 36, 6896 (1996). ( , N. T. Mrabet, J. Van Beeumen, B. Devreese, J. Porath, M. A. Vijayalakshmi. http://dx.doi.org/10.1021/bi9618070)
- 58. V. J. Mol. Recognit. 11, 32 (1998). ( , M. H. Rangeard, N. Mrabet, M. A. Vijayalakshmi. http://dx.doi.org/10.1002/(SICI)1099-1352(199812)11:1/6<32::AID-JMR386>3.0.CO;2-V)
- 59. V. Bioconjug. Chem. 6, 373 (1995). ( , C. Colin, J. Barbet, J. M. Le Doussal, M. A. Vijayalakshmi. http://dx.doi.org/10.1021/bc00034a006)
- 60. H. Electrophoresis 12, 1028 (1991). ( , M. A. Vijayalakshmi. http://dx.doi.org/10.1002/elps.1150121206)
- 61. L. D. Methods 4, 103 (1992). ( , A. A. Serag, S. D. Plunkett, R. J. Todd, F. H. Arnold. http://dx.doi.org/10.1016/1046-2023(92)90061-C)
- 62. T. C. Electrophoresis 1, 67 (1980). ( , K. Takeo. http://dx.doi.org/10.1002/elps.1150010112)
- 63. K. J. Chromatogr., A 698, 89 (1995). ( . http://dx.doi.org/10.1016/0021-9673(94)01265-G)
- 64. W. O. Electrophoresis 17, 489 (1996). ( , K. Haupt, C. Colin, M. A. Vijayalakshmi. http://dx.doi.org/10.1002/elps.1150170310)
- 65. W. O. Biochim. Biophys. Acta 1336, 394 (1997). , M. A. Vijayalakshmi.
- 66. M. V. Bioorg. Khim. 27, 27 (2001). , A. A. Shulga, I. V. Levichkin, M. P. Kirpichnikov, K. M. Poliakov, K. G. Skriabin, M. A. Vijayalakshmi, V. P. Varlamov.
- 67. M. V. J. Mol. Recognit. 19, 287 (2006). ( , W. O. Baek, V. P. Varlamov, N. T. Mrabet, M. A. Vijayalakshmi. http://dx.doi.org/10.1002/jmr.791)
- 68. M. A. J. Capillary Electrophor. 3, 275 (1996). , E. Bossú, H. Engelhardt.
- 69. M. Electrophoresis 21, 909 (2000). ( , M. Cretich, F. Damin, L. Ceriotti, R. Consonni. http://dx.doi.org/10.1002/(SICI)1522-2683(20000301)21:5<909::AID-ELPS909>3.0.CO;2-L)
- 70. K. Y. Biochim. Biophys. Acta 1433, 198 (1999). , O. Pitiot, M. Anissimova, H. Adenier, M. A. Vijayalakshmi.
- 71. P. A. Albertsson. Partition of Cell Particles and Macromolecules, 2nd ed., Almqvist & Wiksell, Stockholm (1971).
- 72. G. J. Chromatogr. 539, 267 (1991). ( , M. A. Vijayalakshmi, T. Stigbrand, G. Kopperschläger. http://dx.doi.org/10.1016/S0021-9673(01)83935-2)
- 73. E. J. Mol. Recognit. 8, 77 (1995). ( , M. A. Vijayalakshmi, K. C. Chadha. http://dx.doi.org/10.1002/jmr.300080114)
- 74. E. J. Mol. Recognit. 10, 262 (1997). ( , M. A. Vijayalakshmi. http://dx.doi.org/10.1002/(SICI)1099-1352(199711/12)10:6<262::AID-JMR377>3.0.CO;2-9)