Abstract
Secondary structural changes of metmyoglobin and apomyoglobin were examined in solutions of sodium alkylsulfates with hydrocarbon numbers of 8 and 12, and alkyltrimethylammonium bromides with hydrocarbon numbers of 10, 12, 14, and 16. The relative proportion ofa-helical structure was estimated by the curve-fitting method of circular dichroic spectrum. The helical proportions of metmyoglobin and apomyoglobin were 82 and 63%, respectively. The shorter the hydrocarbon chain the surfactant had, the higher the concentration necessary to disrupt the secondary structures of these proteins. However, the helical proportion had a tendency to decrease down to lower values in solutions of the cationic surfactants with short hydrophobic groups. On the other hand, thea-helical structure of apomyoglobin was disrupted in lower concentrations of each cationic surfactant than that of metmyoglobin, although the disruptions of the same structures in both the proteins occurred in the same concentration range of each anionic surfactant. It appeared likely that the removal of the heme group unstabilized the myoglobin conformation only in the cationic surfactant solutions.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Breslow, E. (1964).J. Biol. Chem. 239, 486–496.
Breslow, E., Beychok, S., Hardman, K. D., and Guro, F. R. N. (1965).J. Biol. Chem. 240, 304–309.
Brown, J. R. (1977). InAlbumin Structure, Function, and Uses (Rosenoer, V. M., Oratz, M., and Rothschild, M. A., eds.), Pergamon Press, Oxford, pp. 27–51.
Carter, D. C., He, X.-M., Munson, S. H., Twigg, P. D., Gernert, K. M., Broom, M. B., and Miller, T. Y. (1989).Science 244, 1195–1198.
Chen, Y. H., Yang, J. T., and Chau, K. H. (1974).Biochemistry 13, 3350–3359.
Crumpton, M. J., and Wilkinson, J. M. (1965).Biochem. J. 94, 545–556.
Dickerson, R. E. (1964). InThe Proteins (Neurath, H., ed.), Academic Press, New York, Vol., 2, 2nd ed., p. 64.
Edmundson, A. B. (1965).Nature (London) 205, 883–887.
Goto, Y., and Fink, A. L. (1990).J. Mol. Biol. 214, 803–805.
Harrison, S. C., and Blout, E. R. (1965).J. Biol. Chem. 240, 299–303.
Jones, M. N. (1975). InBiological Interfaces, Elsevier, Amsterdam, pp. 101–130.
Kauzmann, W. (1959).Advan. Protein Chem. 14, 1–63.
Kendrew, J. C., Dickerson, R. E., Strandberg, B. E., Hart, R. G., Davies, D. R., Phillips, D. C., and Shore, V. C. (1960).Nature (London) 185, 422–427.
Kendrew, J. C., Watson, H. C., Strandberg, B. E., Dickerson, R. E., Phillips, D. C., and Shore, V. C. (1961).Nature (London) 190, 666–670.
Lapanje, S. (1978). InPhysicochemical Aspects of Protein Denaturation, Wiley-Interscience, New York, pp. 156–179.
Nakano, M., and Yang, J. T. (1981).Arch. Biochem. Biophys. 207, 69–74.
Puett, D. (1973).J. Biol. Chem. 248, 4623–4634.
Stenberg, I. Z., and Sheraga, H. A. (1963).J. Biol. Chem. 238, 172–181.
Steinhardt, J., and Reynolds, J. A. (1969). InMultiple Equilibria in Proteins, Academic Press, New York, pp. 239–302.
Takeda, K., Miura, M., and Takagi, T. (1981).J. Colloid Interface Sci. 82, 38–44.
Takeda, K., and Moriyama, Y. (1990).J. Protein Chem. 9, 573–582.
Takeda, K., and Moriyama, Y. (1991).J. Am. Chem. Soc. 113, 6700–6701.
Takeda, K., Sasa, K., Kawamoto, K., Wada, A., and Aoki, K. (1988a).J. Colloid Interface Sci. 124, 284–289.
Takeda, K., Shigeta, M., and Aoki, K. (1987).J. Colloid Interface Sci. 117, 120–126.
Takeda, K., Wada, A., Nishimura, T., Ueki, T., and Aoki, K. (1989).J. Colloid Interface Sci. 133, 497–504.
Takeda, K., Wada, A., Yamamoto, K., Hachiya, K., and Batra, P. P. (1988b).J. Colloid Interface Sci. 125, 307–313.
Teale, F. W. J. (1959).Biochim. Biophys. Acta 35, 543.
Yonath, J., and Blauer, G. (1974).Eur. J. Biochem. 41, 163–170.
Wada, A., and Takeda, K. (1990).J. Colloid Interface Sci. 138, 277–279.
Watson, H. C. (1969).Progr. Stereochem. 4, 299–333.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Moriyama, Y., Sasaoka, H., Ichiyanagi, T. et al. Secondary structural changes of metmyoglobin and apomyoglobin in anionic and cationic surfactant solutions: Effect of the hydrophobic chain length of the surfactants on the structural changes. J Protein Chem 11, 583–588 (1992). https://doi.org/10.1007/BF01024957
Received:
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF01024957