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Cibacron blue F3G-A and related dyes as ligands in affinity chromatography

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Chromatography

Part of the book series: Advances in Biochemical Engineering ((ABE,volume 25))

Abstract

Cibacron Blue F3G-A and related dyes are sulfonated polyaromatic compounds which bind with considerable specificity and significant affinity to nucleotide-dependent enzymes and to a series of other proteins. After fixation to appropriate insoluble supports, they find wide application as ligands in affinity chromatography.

Initially, the interaction of Cibacron Blue F3G-A with enzymes was regarded as specific because the enzyme-dye complexes were found to be dissociated by low concentrations of competing natural ligands. This gave rise to the assumption that the dye might imitate the conformation of the nucleotide coenzymes and bind specifically to the corresponding nucleotide binding sites of the respective proteins. However, in view of all experimental findings this conception appears too limited. This article describes a more general model of the dye-enzyme interaction in which the dinucleotide binding fold is considered only to be a special case of the postulated specific dye-binding site.

Practical aspects of the application of reactive dyes in affinity chromatography, e.g. choice of the support and of the dye, methods of dye fixation, conditions of binding and elution of enzymes and other proteins are discussed. The international literature which deals with the purification of enzymes and other proteins on a preparative scale by means of chromatography with immobilized dyes as ligands is reviewed. Dye-ligand affinity chromatography has found application in the isolation and purification of a series of dehydrogenases, phosphotransferases, t-RNA- synthetases, restriction endonucleases and initiation factors of protein biosynthesis as well as of plasma proteins like albumin, α1-acid glycoprotein, α-fetoprotein, α1-proteinase inhibitor, clotting factors II and X, and complement factors.

Finally, the possibilities of further research into this field which may give rise to the development of new, perhaps more appropriate, affinity gels will briefly discussed.

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Abbreviations

Fru-6-p:

fructose 6-phosphate

Fru-l,6-p2 :

fructose 1,6-bisphosphate

OMP:

orotidine 5′-monophosphate

Poly A:

polyadenylic acid

Poly C:

polycytidylic acid

Poly G:

polyguanylic acid

Poly I:

polyinosinic acid

8 References

  1. Haff, L. A., Easterday, R. L.: Cibacron Blue-Sepharose: A tool for general ligand affinity chromatography, in: Theory and Practice in affinity chromatography (Eckstein, F., Sundaram, P. V. (eds.)), p. 23. New York, Academic Press 1978

    Google Scholar 

  2. Kopperschläger, G. et al.: FEBS Letters 1, 137 (1968)

    Google Scholar 

  3. Kopperschläger, G.: 5th Ann. Meet. Biochem. Soc. GDR, Berlin, 1969

    Google Scholar 

  4. Haeckel, R. et al.: Hoppe-Seyler's Z. Physiol. Chem. 349, 699 (1968)

    Google Scholar 

  5. Staal, G., Visser, J., Veeger, C: Biochim. Biophys. Acta 185, 39 (1969)

    Google Scholar 

  6. Marshall, J.: J. Chromatogr. 53, 379 (1970)

    Google Scholar 

  7. Aparicio, P. J. et al.: Phytochem. 10, 1487 (1971)

    Google Scholar 

  8. Swart, A. C. W., Kop-Klaassen, B. H. M., Hemker, H. C: Haemostasis 1, 237 (1972/73)

    Google Scholar 

  9. Kopperschläger, G. et al.: Eur. J. Biochem. 22, 40 (1971)

    Google Scholar 

  10. Böhme, H.-J. et al.: J. Chromatogr. 69, 209 (1972)

    Google Scholar 

  11. Kopperschläger, G. et al.: III. Symp. Chromatogr. Clin. Biochem. Leipzig 1971

    Google Scholar 

  12. Röschlau, P., Hess, B.: Hoppe-Seyler's Z. Physiol. Chem. 353, 441 (1971)

    Google Scholar 

  13. Ryan, L. D., Vestling, C. S.: Arch. Biochem. Biophys. 160, 279 (1974)

    Google Scholar 

  14. Stellwagen, E. et al.: Nature 257, 716 (1975)

    Google Scholar 

  15. Weber, B. H. et al.: Biochem. Biophys. Res. Commun. 86, 252 (1979)

    Google Scholar 

  16. Apps, D. K., Gleed, C. D.: Biochem. J. 159, 441 (1976)

    Google Scholar 

  17. Edwards, R. A., Woody, R. W.: Biochem. Biophys. Res. Commun. 79, 470 (1977)

    Google Scholar 

  18. Baird, J. K. et al.: FEBS Letters 70, 61 (1976)

    Google Scholar 

  19. Kopperschläger, G., Böhme, H.-J.: 1st Joint Symp. Biochem. Soc. CSSR and GDR, Reinhards-brunn, 1980

    Google Scholar 

  20. Beissner, R. S., Rudolph, F. B.: Arch. Biochem. Biophys. 189, 76 (1978)

    Google Scholar 

  21. Thompson, S. T., Stellwagen, E.: Proc. US-Natl. Acad. Sci. 73, 361 (1976)

    Google Scholar 

  22. Dean, P. D. G., Watson, D. H.: J. Chromatogr. 105, 301 (1979)

    Google Scholar 

  23. Böhme, H.-J. et al.: Acta biol. med. germ. 34, 1447 (1975)

    Google Scholar 

  24. Chambers, G. K.: Anal. Biochem. 83, 551 (1977)

    Google Scholar 

  25. Angal, S., Dean, P. D. G.: Biochem. J. 167, 301 (1977)

    Google Scholar 

  26. Blume, K. G. et al.: Biochim. Biophys. Acta 227, 364 (1971)

    Google Scholar 

  27. Thompson, S. T., Cass, K. H., Stellwagen, E.: Proc. US-Natl. Acad. Sci. 72, 669 (1975)

    Google Scholar 

  28. Kobayashi, R., Fang, V. S.: Biochem. Biophys. Res. Commun. 69, 1080 (1976)

    Google Scholar 

  29. Wilson, J. E.: ibid. 72, 816 (1976)

    Google Scholar 

  30. Schuber, F., Pascal, M.: Biochimie 59, 735 (1977)

    Google Scholar 

  31. Ashton, A. R., Polya, G. M.: Biochem. J. 175, 501 (1978)

    Google Scholar 

  32. Böhme, H.-J. et al.: Acta biol. med. germ. 37, 173 (1978)

    Google Scholar 

  33. Beissner, R. S., Rudolph, F. B.: J. Chromatogr. 161, 127 (1978)

    Google Scholar 

  34. Stellwagen, E.: J. Mol. Biol. 106, 903 (1976)

    Google Scholar 

  35. Grazi, E. et al.: Arch. Biochem. Biophys. 190, 405 (1978)

    Google Scholar 

  36. Watson, D. H., Harvey, J. M., Dean, D. G. P.: Biochem. J. 173, 591 (1978)

    Google Scholar 

  37. Stockton, J. et al.: Biochem. Soc. Trans. 6, 200 (1978)

    Google Scholar 

  38. Cottreau, D., Levin, M. J., Kahn, A.: Biochim. Biophys. Acta 568, 183 (1979)

    Google Scholar 

  39. Edwards, R. E., Woody, R. W.: Biochemistry 18, 5197 (1979)

    Google Scholar 

  40. Travis, J., Pannell, R.: Clin. Chim. Acta 49, 49 (1973)

    Google Scholar 

  41. Beissner, R. S., Quiocho, F. A., Rudolph, F. B.: J. Mol. Biol. 134, 847 (1979)

    Google Scholar 

  42. Biellmann, J. F. et al.: Eur. J. Biochem. 102, 107 (1979)

    Google Scholar 

  43. Bornmann, L., Hess, B.: Z. Naturforsch. 32, 756 (1977)

    Google Scholar 

  44. Glazer, A. N.: Proc. US-Natl. Acad. Sci. 65, 1057 (1970)

    Google Scholar 

  45. Maroya, N. et al.: J. Biochem. 79, 203 (1976)

    Google Scholar 

  46. Kahn, A. et al.: Biochim. Biophys. Acta 523, 59 (1978)

    Google Scholar 

  47. Righetti, P. G., Caravaggio, T.: J. Chromatogr. 127, 1 (1976)

    Google Scholar 

  48. Fischer, S. E., Whitt, G. S.: Anal. Biochem. 94, 89 (1979)

    Google Scholar 

  49. Birkenmeier, G., Ph. D. Thesis: Section of Medicine, Wechselwirkung von Serumproteinen mit trägerfixiertem Cibacronblau F3G-A und anderen Triazinfarbstoffen, Karl-Marx-Univers. Leipzig 1981, J. Chromatogr. in press

    Google Scholar 

  50. Cuatrecasas, P., Wilchek, M., Anfinsen, C. B.: Proc. US-Natl. Acad. Sci. 61, 636 (1968)

    Google Scholar 

  51. Heyns, W., DeMoor, P.: Biochim. Biophys. Acta 358, 1 (1974)

    Google Scholar 

  52. Leatherbarrow, J., Dean, D. G.: Biochem. J. 189, 27 (1980)

    Google Scholar 

  53. Mislovićova, D. et al.: J. Chromatogr. 194, 95 (1980)

    Google Scholar 

  54. Anderson, P. A., Jervis, L.: Biochem. Soc. Trans. 6, 263 (1978)

    Google Scholar 

  55. Meldolesi, M. F., Macchia, V., Laccetti, P.: J. Biol. Chem. 251, 6244 (1977)

    Google Scholar 

  56. Lowe, C. R. et al.: Anal. Biochem. 104, 23 (1980)

    Google Scholar 

  57. Harris, N. D., Byfield, P. G. H.: FEBS Lett. 103, 162 (1979)

    Google Scholar 

  58. Hagele, E., Neeff, J., Mecke, D.: Eur. J. Biochem. 83, 67 (1978)

    Google Scholar 

  59. Hofmann, E., Kopperschläger, G.: Phosphofructokinase, Yeast, in: Methods in Enzymology: (Colowick, S. P., Kaplan, N. O. (eds.)), New York, Academic Press (in press)

    Google Scholar 

  60. Khang, N. Q., Böhme, H.-J., Hofmann, E.: Acta biol. med. germ. 36, 1019 (1977)

    Google Scholar 

  61. Khang, N. Q., Böhme, H.-J., Hofmann, E.: ibid. 35, 1425 (1976)

    Google Scholar 

  62. Easterday, R. L., Easterday, J. M.: Adv. Exp. Med. Biol. 42, 123 (1974)

    Google Scholar 

  63. Bollin, E. et al.: Prep. Biochem. 8, 259 (1978)

    Google Scholar 

  64. Pompon, D., Lederer, F.: Eur. J. Biochem. 90, 563 (1978)

    Google Scholar 

  65. Pompon, D., Guiard, B., Lederer, F.: ibid. 110, 565 (1980)

    Google Scholar 

  66. Edwards, P., Lemongello, D., Fogelman, A.: Fed. Proc. 37, 1524 (1978)

    Google Scholar 

  67. Reyes, P., Sandquist, R.: Anal. Biochem. 88, 522 (1978)

    Google Scholar 

  68. Marie, J., Kahn, A.: Enzyme 22, 407 (1977)

    Google Scholar 

  69. Drocourt, J.-L., Thang, D.-Ch., Thang, M. N.: Eur. J. Biochem. 82, 355 (1978)

    Google Scholar 

  70. Wille, L. E.: Clin. Chem. Acta 71, 355 (1976)

    Google Scholar 

  71. Travis, J. et al.: Biochem. J. 157, 301 (1976)

    Google Scholar 

  72. Erickson, J. S., Paucker, K.: Anal. Biochem. 98, 214 (1979)

    Google Scholar 

  73. Morgan, M. R. A. et al.: FEBS Lett. 87, 239 (1978)

    Google Scholar 

  74. Bostian, K. A., Betts, G. F.: Biochem. J. 173, 773 (1978)

    Google Scholar 

  75. Adinolfi, A., Hopkinson, D. A.: Ann. Human. Genetics 41, 399 (1978)

    Google Scholar 

  76. Nadal-Ginard, B., Markert, C.: Use of affinity chromatography for purification of lactate dehydrogenase and for assessing the homology and function of the A and B subunits, in: Isoenzymes, Vol. I, p. 45, New York, Academic Press 1975

    Google Scholar 

  77. Gordon, G. L., Doelle, H. W.: Eur. J. Biochem. 67, 543 (1976)

    Google Scholar 

  78. Kuan, K. N., Jones, G. L., Vestling, C. S.: Biochemistry 18, 4366 (1979)

    Google Scholar 

  79. Böhme, H.-J., Kopperschlager, G.: unpublished

    Google Scholar 

  80. Chambers, B. B., Dunlap, R. B.: J. Biol. Chem. 254, 6515 (1979)

    Google Scholar 

  81. Kawai, K., Eguchi, Y.: J. Ferm. Tech. 54, 609 (1976)

    Google Scholar 

  82. Kawagishi, T. et al.: Agric. Biol. Chem. 44, 949 (1980)

    Google Scholar 

  83. Viowanath-Reddy, M., Pyle, J. E., Howe, H. B., Jr.: J. Gen. Microbiol. 107, 289 (1978)

    Google Scholar 

  84. Gärtner, G.: Ph. D. Thesis: Reinigung und Charakterisierung der Glyceroldehydrogenase aus Candida valida, Karl-Marx-Univers. Leipzig 1981

    Google Scholar 

  85. Cass, K. H., Stellwagen, E.: Arch. Biochem. Biophys. 171, 682 (1975)

    Google Scholar 

  86. Kotlarz, D., Buc, H.: Biochim. Biophys. Acta 484, 35 (1977)

    Google Scholar 

  87. Simon, W. A., Hofer, H. W.: ibid. 481, 450 (1977)

    Google Scholar 

  88. Witt, J. J., Roskowski, R.: Biochemistry 14, 4503 (1975)

    Google Scholar 

  89. Demaille, J. G., Peters, K. A., Fischer, E. H.: ibid. 16, 3080 (1977)

    Google Scholar 

  90. Armstrong, R. N. et al.: Biochemistry 18, 1230 (1979)

    Google Scholar 

  91. Moe, J. G., Piszkiewicz, D.: FEBS Lett. 72, 147 (1976)

    Google Scholar 

  92. Nikodem, V. M., Johnson, R. C, Fresco, J. R.: Fed. Proc. 36, 822 (1977)

    Google Scholar 

  93. Sugiura, M.: Anal. Biochem. 108, 227 (1980)

    Google Scholar 

  94. Baksi, K., Rogerson, D. L., Rushizky, G. W.: Biochemistry 17, 4136 (1978)

    Google Scholar 

  95. Baksi, K., Rushizky, G. W.: Fed. Proc. 37, 1414 (1978)

    Google Scholar 

  96. Baksi, K., Rushizky, G. W.: Anal. Biochem. 99, 207 (1979)

    Google Scholar 

  97. Baksi, K., Rushizky, G. W.: Fed. Proc. 38, 486 (1979)

    Google Scholar 

  98. Manual Amicon Corporation: Dye-Ligand Chromatography, Amicon Corp., Lexington 1980

    Google Scholar 

  99. Dean, P. D. G. et al.: Biochem. Soc. Trans. 5, 1111 (1977)

    Google Scholar 

  100. Iqbal, M. J., Johnson, M. W.: Ster. Biochem. 8, 977 (1977)

    Google Scholar 

  101. Angal, S., Dean, P. D. G.: FEBS Lett. 96, 346 (1978)

    Google Scholar 

  102. Pannell, R., Johnson, D., Travis, J.: Biochemistry 13, 5439 (1974)

    Google Scholar 

  103. Kelleher, P. C, Smith, C. J., Pannell, R.: J. Chromatogr. 173, 415 (1979)

    Google Scholar 

  104. Young, J. C, Webb, B. A.: Anal. Biochem. 88, 619 (1978)

    Google Scholar 

  105. Wu, J. T., Wu, L. H., Madsen, A. C: Biochem. Med. 23, 336 (1980)

    Google Scholar 

  106. Clarke, L. E., Slade, B. S.: J. Reprod. Immun. 2, 109 (1980)

    Google Scholar 

  107. Travis, J., Garner, D., Bowen, J.: Biochemistry 17, 5647 (1978)

    Google Scholar 

  108. Vician, L., Tishkoff, G.: Biochim. Biophys. Acta 434, 199 (1976)

    Google Scholar 

  109. Gee, A. P., Borsos, T., Boyle, M. D. P.: J. Immun. Methods 30, 119 (1979)

    Google Scholar 

  110. Jankowski, W. J. et al.: Biochemistry 15, 5182 (1976)

    Google Scholar 

  111. DeMaeyer-Guignard, J., Thang, M. N., DeMaeyer, E.: Proc. US-Natl. Acad. Sci. 74, 3787 (1977)

    Google Scholar 

  112. Wu, J. M.: FEBS Lett. 110, 297 (1980)

    Google Scholar 

  113. Kristensen, T., Holthund, J.: J. Chromatogr. 192, 494 (1980)

    Google Scholar 

  114. Toste, A. P., Cooke, R.: Anal. Biochem. 95, 317 (1979)

    Google Scholar 

  115. Reisler, E. et al.: Biochim. Biophys. Acta 623, 243 (1980)

    Google Scholar 

  116. Barlow, C. F., Firemark, H., Roth, L. J.: J. Phar. Pharm. 9, 550 (1962)

    Google Scholar 

  117. Glazer, A. N.: J. Biol. Chem. 242, 3326 (1967)

    Google Scholar 

  118. Weiner, H. W., Koshland, D. E. Jr.: J. Biol. Chem. 240, PC 2764 (1965)

    Google Scholar 

  119. Bernhard, S. A., Lee, B. F., Tashjian, Z. H.: J. Mol. Biol. 18, 405 (1966)

    Google Scholar 

  120. Glazer, A. N.: J. Biol. Chem. 242, 4528 (1967)

    Google Scholar 

  121. Varpholomeev, S. D., Martinek, K., Berezin, I. V.: Mol. Biol. (Russian) 6, 148 (1972)

    Google Scholar 

  122. Heitz, J. R., Brand, L.: Biochemistry 10, 2695 (1971)

    Google Scholar 

  123. Kvamme, E., Tveit, B., Sveneby, G.: Biochem. Biophys. Res. Commun. 20, 566 (1965)

    Google Scholar 

  124. Ullmann, A., Vagelos, P. R., Monod, J.: Biochem. Biophys. Res. Commun. 17, 86 (1964)

    Google Scholar 

  125. Lamkin, G. E., King, E. E.: Biochem. Biophys. Res. Commun. 72, 560 (1976)

    Google Scholar 

  126. Roy, S. K., Nishikawa, A. H.: Biotech. Bioeng. 21, 775 (1979)

    Google Scholar 

  127. Bauermeister, A., Sargent, J.: Biochem. Soc. Trans. 6, 222 (1978)

    Google Scholar 

  128. Boghosian, R. A., McGuinness, E. T.: Biochim. Biophys. Acta 567, 278 (1979)

    Google Scholar 

  129. Tamaki, N. et al.: J. Biochem. 82, 73 (1977)

    Google Scholar 

  130. Turner, A. J., Hryszko, J.: Biochim. Biophys. Acta 613, 256 (1980)

    Google Scholar 

  131. Chauvin, M. M. et al.: Can. J. Biochem. 57, 178 (1979)

    Google Scholar 

  132. Dao, M. L. et al.: J. Biol. Chem. 254, 9441 (1979)

    Google Scholar 

  133. Ben-Bassat, A., Goldberg, J. Biochim. Biophys. Acta 611, 1 (1980)

    Google Scholar 

  134. Ruch, F. E. Jr. et al.: J. Bacteriol. 141, 1077 (1980)

    Google Scholar 

  135. Tormanen, C. D. et al.: Biochem. Biophys. Res. Commun. 68, 754 (1976)

    Google Scholar 

  136. Srikantaiah, M. V. et al.: J. Biol. Chem. 252, 6145 (1977)

    Google Scholar 

  137. Ness, G., Spindler, C, Moffler, M.: Fed. Proc. 38, 672 (1979)

    Google Scholar 

  138. Beg, Z. H., Stonik, J. A., Brewer, H. B.: FEBS Lett. 80, 123 (1977)

    Google Scholar 

  139. Westbrook, C, Lin, Y. M., Jarabak, J.: Biochem. Biophys. Res. Commun. 76, 943 (1977)

    Google Scholar 

  140. Lin, Y. M., Jarabak, J.: ibid. 81, 1227 (1978)

    Google Scholar 

  141. Seelig, G. F., Colman, R. F.: J. Biol. Chem. 252, 3671 (1977)

    Google Scholar 

  142. Vasquez, B., Reeves, H..C: Biochim. Biophys. Acta 578, 31 (1979)

    Google Scholar 

  143. Garnak, M., Reeves, H. C: J. Biol. Chem. 254, 7915 (1979)

    Google Scholar 

  144. Nagaoka, T. et al.: J. Biochem. 81, 71 (1977)

    Google Scholar 

  145. Kawai, K., Saito, Y., Eguchi, Y.: J. Ferment. Technol. 58, 569 (1980)

    Google Scholar 

  146. Anderson, P. A., Jervis, L.: Biochem. Soc. Trans. 5, 728 (1977)

    Google Scholar 

  147. Barthova, J., Pecka, M., Leblova, S.: Coll. Czech. Chem. Commun. 42, 3705 (1977)

    Google Scholar 

  148. Guerrero, M. G., Jetschmann, K., Volker, W.: Biochim. Biophys. Acta 482, 19 (1977)

    Google Scholar 

  149. Guerrero, M. G., Gutierrez, M.: ibid. 482, 272 (1977)

    Google Scholar 

  150. Notton, B. A., Fido, R. J., Hewitt, E. J.: Plant Sci. Ltrs. 8, 165 (1977)

    Google Scholar 

  151. Greenbaum, P., Prodouz, K. N., Garrett, R. H.: Biochim. Biophys. Acta 526, 52 (1978)

    Google Scholar 

  152. Amy, N. K.., Garrett, R. H., Anderson, B. M.: ibid. 480, 83 (1977)

    Google Scholar 

  153. Van der Jagt, D.L., Davidson, L. M.: ibid. 484, 260 (1977)

    Google Scholar 

  154. Pannell, R., Newmann, R.: Fed. Proc. 37, 1528 (1978)

    Google Scholar 

  155. DeAbreu, R. A., DeKok, A., Veeger, C: FEBS Lett. 82, 89 (1977)

    Google Scholar 

  156. Barea, J., Giles, N. H.: Biochim. Biophys. Acta 524, 1 (1978)

    Google Scholar 

  157. Polley, L. D.: ibid. 526, 259 (1978)

    Google Scholar 

  158. Cheng, Y.-C, Domin, B.: Anal. Biochem. 85, 425 (1978)

    Google Scholar 

  159. Itakura, T. et al.: Eur. J. Biochem. 82, 431 (1978)

    Google Scholar 

  160. Baxter, A., Currie, L. M., Durham, J.P.: Biochem. J. 173, 1005 (1978)

    Google Scholar 

  161. Deibel, M. R., Ives, D. H.: J. Biol Chem. 252, 8235 (1977)

    Google Scholar 

  162. Kagimoto, T., Uyeda, K.: ibid. 254, 5584 (1979)

    Google Scholar 

  163. Meldolesi, M. F., Macchia, V., Laccetti, P.: ibid. 251, 6244 (1976)

    Google Scholar 

  164. Thornbergh, B. N., Wu, L. L., Griffin, Ch. C: Can. J. Biochem. 56, 836 (1978)

    Google Scholar 

  165. Ewings, K. N., Doelle, H. W.: Eur. J. Biochem. 69, 563 (1976)

    Google Scholar 

  166. Akkerman, J. W. et al.: Biochim. Biophys. Acta 370, 102 (1974)

    Google Scholar 

  167. Yamada, T., Ohyama, H.: ibid. 284, 101 (1972)

    Google Scholar 

  168. Diezel, W. et al.: Eur. J. Biochem. 38, 479 (1973)

    Google Scholar 

  169. Tamaki, N., Hess, B.: Hoppe-Seyler's Z. Physiol. Chem. 356, 399 (1975)

    Google Scholar 

  170. Kulbe, K. D., Schuer, R.: Anal. Biochem. 93, 46 (1979)

    Google Scholar 

  171. Kawai, K., Eguchi, Y.; J. Ferment. Technol. 58, 383 (1980)

    Google Scholar 

  172. Cavell, S., Scopes, R. K.: Eur. J. Biochem. 63, 483 (1976)

    Google Scholar 

  173. Nichols, B. P. et al.: Biochim. Biophys. Acta 526, 410 (1978)

    Google Scholar 

  174. Pai, S. H. et al.: Eur. J. Biochem. 55, 299 (1975)

    Google Scholar 

  175. Staal, G. E. J. et al.: Biochim. Biophys. Acta 227, 88 (1971)

    Google Scholar 

  176. Marie, J., Kahn, A., Boivin, P.: ibid. 481, 96 (1977)

    Google Scholar 

  177. Markins, R. W., Black, J. A., Rittenberg, M. B.: Biochemistry 16, 3831 (1977)

    Google Scholar 

  178. Zimmermann, J., Fern, M.: Fed. Proc. 38, 673 (1979)

    Google Scholar 

  179. Morelli, J., Kayne, F. J.: ibid. 36, 718 (1977)

    Google Scholar 

  180. Riou, J. R., Claus, T. H., Pilkins, S. J.: J. Biol. Chem. 253, 656 (1978)

    Google Scholar 

  181. Solomonson, L., Plant Physiol. 56, 853 (1975)

    Google Scholar 

  182. Stellwagen, E., Baker, B.: Nature 261, 719 (1976)

    Google Scholar 

  183. Markham, G. D., Reed, G. H.: Arch. Biochem. Biophys. 184, 24 (1977)

    Google Scholar 

  184. Kirchberger, J., Kopperschläger, G.: unpublished

    Google Scholar 

  185. Gaertner, F. H., Cole, K. W.: Arch. Biochem. Biophys. 177, 566 (1976)

    Google Scholar 

  186. Kido, H., Vita, A., Horecker, B. L.: Anal. Biochem. 106, 450 (1980)

    Google Scholar 

  187. Ahmad, A., Surolio, A., Bachhawat, B. K.: Biochim. Biophys. Acta 481, 542 (1977)

    Google Scholar 

  188. Rose, Z. B., Dube, S.: Arch. Biochem. Biophys. 177, 284 (1976)

    Google Scholar 

  189. Mori, M., Cohen, P.: Fed. Proc. 37, 1341 (1978)

    Google Scholar 

  190. Roskoski, R. Jr., Lim, C. T. L., Roskoski, L.: Biochemistry 14, 5105 (1975)

    Google Scholar 

  191. Morrill, M., Thompson, S. T., Stellwagen, E.: J. Biol. Chem. 254, 4371 (1979)

    Google Scholar 

  192. Lepo, J. E. et al.: Biochim. Biophys. Acta 568, 428 (1979)

    Google Scholar 

  193. Silink, M. et al.: J. Biol. Chem. 250, 5982 (1975)

    Google Scholar 

  194. Uotila, L., Koivusalo, M.: Eur. J. Biochem. 52, 493 (1975)

    Google Scholar 

  195. Elango, N., Janaki, I., Rav, A. R.: Biochem. Biophys. Res. Commun. 83, 1388 (1978)

    Google Scholar 

  196. Sekura, R. D., Jakoby, W. B.: J. Biol. Chem. 254, 5658 (1979)

    Google Scholar 

  197. Oka, J., Ueda, K., Havaishi, O.: Biochem. Biophys. Res. Commun. 80, 841 (1978)

    Google Scholar 

  198. Mandel, P., Okazaki, H., Niedergang, C: FEBS Lett. 84, 331 (1977)

    Google Scholar 

  199. Deibel, M. R., Coleman, M.: J. Biol. Chem. 254, 8634 (1979)

    Google Scholar 

  200. Whittle, S., Turner, A.: J. Neurochem. 6, 1453 (1978)

    Google Scholar 

  201. Turner, A. J., Pearson, A. G. M., Mason, R. J.: Studies on methylenetetrahydrofolate reductase from ox brain, in: Chemistry and Biology of Pteridines (E. Brown (ed.)), p. 501, Amsterdam, Elsevier 1980

    Google Scholar 

  202. Williamson, J. H., Krochko, D., Bentley, M. M.: Comp. Biochem. Physiol. 65B, 339 (1980)

    Google Scholar 

  203. Virca, G. D. et al.: Anal. Biochem. 89, 274 (1978)

    Google Scholar 

  204. Van der Mast, C., Voorna, H.O.: Biochim. Biophys. Acta 601, 512 (1980)

    Google Scholar 

  205. Rock, C. D., Cronan, J. E.: J. Biol. Chem. 254, 7116 (1979)

    Google Scholar 

  206. Robinson, Jr. et al.: Proc. US-Natl. Acad. Sci. 77, 5847 (1980)

    Google Scholar 

  207. Robinson, Jr., J.B., Strottmann, J. M., Stellwagen, E.: ibid. 78, 2287 (1981)

    Google Scholar 

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  1. Institute of Physiological Chemistry, Karl-Marx-University Leipzig, 7010, Leipzig, DDR

    Gerhard Kopperschläger, Hans-Joachim Böhme & Eberhard Hofmann

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  1. Gerhard Kopperschläger
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  2. Hans-Joachim Böhme
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  3. Eberhard Hofmann
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A. Fiechter

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© 1982 Springer-Verlag

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Kopperschläger, G., Böhme, HJ., Hofmann, E. (1982). Cibacron blue F3G-A and related dyes as ligands in affinity chromatography. In: Fiechter, A. (eds) Chromatography. Advances in Biochemical Engineering, vol 25. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3540118292_4

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  • DOI: https://doi.org/10.1007/3540118292_4

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  • Print ISBN: 978-3-540-11829-9

  • Online ISBN: 978-3-540-39495-2

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