Neurochemical Research

, Volume 12, Issue 5, pp 409–417 | Cite as

The association of myelin basic protein with itself and other proteins

  • John E. Moskaitis
  • Lisa C. Shriver
  • Anthony T. Campagnoni
Original Articles

Abstract

Chromatographic studies were performed to measure myelin basic protein (MBP) interactions by covalently binding a number of different proteins to Sepharose and passing radioactive bovine MBP over these columns. Studies at a variety of pH values, ionic strengths and temperatures revealed that the bovine MBP could interact with itself as well as cytochrome c, lysozyme, and ovalbumin. Chromatographic profiles of elution volume vs. pH revealed that the interaction between MBP and these immobilized proteins was biphasic. The self-association of MBP was found to be strongest between pH 7.4 and 8.1 and at an elevated temperature. Titration of the amino acid residues responsible for the association of MBP with other proteins revealed apparent pKs ranging from 6.10 to 6.70. A pH dependence study at an elevated temperature shifted the apparent pK of the MBP interaction to a lower value with all the proteins except ovalbumin. After destroying 60% of the histidine residues in MBP by photooxidation and passing125I-labeled photooxidized MBP over Sepharose columns containing immobilized protein, the second phase in binding was decreased significantly with immobilized cytochrome c, lysozyme, and MBP and to a smaller extent with ovalbumin. These results are consistent with the involvement of deprotonated histidine residues in the MBP-protein associations.

Key Words

Myelin basic protein protein-protein interactions affinity chromatography 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Crang, A. J., and Rumsoy, M. G. 1977. The labeling of lipid and protein components in isolated central nervous system myelin with dansyl chloride. Biochem. Soc. Trans. 5:110–112.Google Scholar
  2. 2.
    Rumsby, M. G. and Crang, A. J. 1977. The myelin sheath—a structural examination. Pages 247–362, in Poste, G. and Nicholson, G. L. (eds). Cell Surface Reviews, Vol. 4 North Holland, New York.Google Scholar
  3. 3.
    Carnegie, P. R., and Moore, W. J. 1980. Myelin basic protein. Pages 120–143, in Bradshaw, A. and Schneider, M. (eds.), Proteins of the nervous system. Raven Press, New York.Google Scholar
  4. 4.
    Braun, P. E. 1977. Molecular architecture of myelin. Pages 91–115, in Morell, P. (ed.), Myelin. Plenum Press, New York.Google Scholar
  5. 5.
    Boggs, J. M., Moscarello, M. A., and Papahadjopoulos, D. 1982. Structural organization of myelin—Role of lipid-protein interactions determined in model systems. Pages 1–51, in Jost, P. C. and Griffith, O. H. (eds.), Lipid protein interactions, Vol. 2. John Wiley and Sons, New York.Google Scholar
  6. 6.
    Smith, R. 1982. Self-association of myelin basic protein: Enhancement by detergents and lipids. Biochemistry 21:2697–2701.Google Scholar
  7. 7.
    Burns, P. F., Campagnoni, C. W., Chaiken, I. M., and Campagnoni, A. T. 1981. Interactions of free and immobilized myelin basic protein with anionic detergents. Biochemistry 20:2463–2469.Google Scholar
  8. 8.
    Lampe, P. D., Wei, G. J., and Nelsestuen, G. L. 1983. Stopped-flow studies of myelin basic protein association with phospholipid vesicles and subsequent vesicle aggregation. Biochemistry 22:1594–1599.Google Scholar
  9. 9.
    Golds, E. E., and Braun, P. E. 1978. Protein associations and basic protein conformation in the myelin membrane. The use of difluorodinitrobenzene as a cross-linking reagent. J. Biol. Chem. 253:8162–8170.Google Scholar
  10. 10.
    Golds, E. E., and Braun, P. E. 1978. Cross-linking studies on the conformation and dimerization of myelin basic protein in solution. J. Biol. Chem. 253:8171–8177.Google Scholar
  11. 11.
    Smith, R. 1980. Sedimentation analysis of the self-association of bovine myelin basic protein. Biochemistry 19:1826–1831.Google Scholar
  12. 12.
    Smith, R. 1977. Non-covalent cross-linking of lipid bilayers by myelin basic protein. A possible role in myelin formation. Biochim. Biophys. Acta. 470:170–184.Google Scholar
  13. 13.
    Smith, R. 1977. The secondary structure of myelin basic protein extracted by deoxycholate. Biochim. Biophys. Acta 491:581–590.Google Scholar
  14. 14.
    Boggs, J. M., and Moscarello, M. A. 1978. Effect of basic protein from human central nervous system myelin on lipid bilayer structure. J. Membrane Biol. 39:75–96.Google Scholar
  15. 15.
    Lampe, P. D., and Nelsestuen, G. L. 1982. Myelin basic protein-enhanced fusion of membranes. Biochim. Biophys. Acta 693:320–325.Google Scholar
  16. 16.
    Liebes, L. F., Zand, R., and Phillips, W. D. 1975. Solution behavior, circular dichroism and 220 MHz PMR studies of the myelin basic protein. Biochim. Biophys. Acta 504:27–39.Google Scholar
  17. 17.
    Chapman, B. E., and Moore, W. J. 1976. Conformation of myelin basic protein in aqueous solution from nuclear magnetic resonance spectroscopy. Biochem. Biophys. Res. Commun. 73:758–766.Google Scholar
  18. 18.
    Smith, R., and McDonald, B. J. 1979. Association of myelin basic protein with detergent micelles. Biochim. Biophys. Acta. 554:133–147.Google Scholar
  19. 19.
    Reidl, L. S., Campagnoni, C. W., and Campagnoni, A. T. 1981. Preparation and properties of an immunosorbent column specific for the myelin basic protein. J. Neurochem. 37:373–380.Google Scholar
  20. 20.
    Barylko, B., and Dobrowolski, Z. 1984. Ca2+-camodulindependent regulation of F-actin-myelin basic protein interaction. Eur. J. Cell. Biol. 35:327–335.Google Scholar
  21. 21.
    Campagnoni, A. T., Whitehead, D. L., and Rowan, R., III. 1978. Nuclear magnetic resonance studies of myelin basic proteins. Pages 413–421, in Agris, P. F., Loeppky, R. M., and Sykes, B. D. (eds.), Biomolecular structure and function. Academic Press, New York.Google Scholar
  22. 22.
    Campagnoni, C. W., Carey, G. D., and Campagnoni, A. T. 1978. Synthesis of myelin proteins in the developing mouse brain. Arch. Biochem. Biophys. 190:118–125.Google Scholar
  23. 23.
    Craig, L. C. 1967. Techniques for the study of peptides and proteins by dialysis and diffusion. Pages 870–905, in Hirs, C. H. W. (ed.), Methods in Enzymology, Vol 11, Academic Press, New York.Google Scholar
  24. 24.
    Panyim, S., and Chalkley, R. 1969. High resolution acrylamide gel electrophoresis of histones. Arch. Biochem. Biophys. 130:337–346.Google Scholar
  25. 25.
    Weber, K., and Osborn, M. 1969. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244:4406–4412.Google Scholar
  26. 26.
    Elliott, J. I., and Brewer, J. M. 1979. The relation of photooxidized histidines in yeast enolase to enzymatic activity. Arch. Biochem. Biophys. 192:203–213.Google Scholar
  27. 27.
    Cuatrecasas, P., and Anfinsen, C. G. 1971. Affinity chromatography. Pages 345–378, in Jakoby, W. B. (ed.), Methods in Enzymology, Vol 22. Academic Press, New York.Google Scholar
  28. 28.
    Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265–275.Google Scholar
  29. 29.
    Havekes, L., Buckmann, F., and Visser, J. 1974. Immobilized glutamate dehydrogenase: Some catalytic and structural aspects. Biochim. Biophys. Acta 334:272–286.Google Scholar
  30. 30.
    Failla, D., and Santi, D. V. 1973. A simple method for quantitating ligands covalently bound to agarose beads. Anal. Biochem. 52:363–368.Google Scholar
  31. 31.
    Haworth, W. N., and Jones, W. G. M. 1944. The conversion of sucrose into furan compounds. Part I. 5-Hydroxymethylfurfuraldehyde and some derivatives. J. Chem. Soc. 81:667–670.Google Scholar
  32. 32.
    Jencks, W. P. 1959. Studies on the mechanism of oxime and semicarbazone formation. J. Amer. Chem. Soc. 81:475–481.Google Scholar
  33. 33.
    Koelsch, R., Lasch, J., Marquardt, I., and Hanson, H. 1975. Application of spectrophotometric methods to the determination of protein bound to agarose beads. Anal. Biochem. 66:556–567.Google Scholar
  34. 34.
    Chapman, B. E., Littlemore, L. T., and Moore, W. J. 1978. Conformation of myelin basic protein and its role in myelin formation. Pages 207–220, in Palo J. (ed.), Myelination and demyelination. Plenum Press, New York.Google Scholar
  35. 35.
    Boggs, J. M., and Moscarello, M. A. 1978. Structural organization of the human myelin membrane. Biochim. Biophys. Acta 515:1–21.Google Scholar
  36. 36.
    Davison, A., 1970. Myelination pp. 80–161. The biochemistry of the myelin sheath. Pages 50–161, in Kugelmass, I. N. (ed.), Myelination. Charles C. Thomas, Springfield, IL.Google Scholar
  37. 37.
    Greenstein, J. P. 1933. Studies of the peptides of trivalent amino acids. J. Biol. Chem. 101:603–621.Google Scholar
  38. 38.
    Nozaki, Y., and Tanford, C. 1971. The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions: Establishment of a hydrophobicity scale. J. Biol. Chem. 246:2211–2217.Google Scholar

Copyright information

© Plenum Publishing Corporation 1987

Authors and Affiliations

  • John E. Moskaitis
    • 1
  • Lisa C. Shriver
    • 1
  • Anthony T. Campagnoni
    • 1
  1. 1.Department of ChemistryUniversity of MarylandCollege Park

Personalised recommendations