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AUotopic Properties of Human Brain Monoamine Oxidase

Abstract

A NUMBER of preparations of monoamine oxidase (monoamine: O2 oxidoreductase (deaminating) E.C.1.4.3.4.) (MAO) have been shown to contain multiple forms of the enzyme which differ in their electrophoretic mobilities1, 2, inhibitor sensitivities3–5, thermal stabilities6 and, in some cases, immunological properties7–8. Little is known about the nature of these multiple forms although it has been suggested that they might be protein conformers9. The possibility that they might arise from the binding of different amounts or types of lipid material to a single enzyme species is, however, supported by the observation that the electrophoretically separable forms of rat liver MAO contain widely different amounts of phospholipid5, 10. In addition we have recently shown that treatment of a preparation of rat liver monoamine oxidase with the chaotropic agent sodium perchiorate seemed to render the enzyme homogeneous by a number of criteria without any significant loss of activity10. This treatment was shown to be accompanied by the release of lipid material from the enzyme preparation and, since chaotropic agents are known to weaken hydrophobic bonds between protein and lipid11, these results gave further support to the view that the multiple forms are caused by the association of lipid membrane material with a single enzyme.

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References

  1. Youdim, M. B. H., Collins, G. G. S., and Sandler, M., Fed. Eur. Biochem. Soc. Symp., 18, 281 (1970).

    Google Scholar 

  2. Diaz Borges, J. M., and D'lorio, A., Adv. Biochem. Psychopharmac., 5, 79 (1972).

    CAS  Google Scholar 

  3. Hall, D. W. R., Logan, B. W., and Parsons, G. H., Biochem. Pharmac., 18, 1447 (1969).

    CAS  Article  Google Scholar 

  4. Squires, R. F., Adv. Biochem. Psychopharmac., 5, 355 (1972).

    CAS  Google Scholar 

  5. Tipton, K. F., Adv. Biochem. Psychopharmac., 5, 11 (1972).

    CAS  Google Scholar 

  6. Oswald, E. O., and Strittmatter, C. F., Proc Soc. exp. Biol. Med., 114, 668 (1963).

    CAS  Article  Google Scholar 

  7. Hartman, B. K., Biol. Psych., 4, 147 (1972).

    CAS  Google Scholar 

  8. McCauley, R., and Racker, E., Molec. Cell. Biochem., 1, 73 (1973).

    CAS  Article  Google Scholar 

  9. Collins, G. G. S., Sandler, M., Williams, E. D., and Youdim, M. B. H., Nature, 225, 817 (1970).

    CAS  Article  Google Scholar 

  10. Houslay, M. D., and Tipton, K. F., Biochem. J., 135, 173 (1973).

    CAS  Article  Google Scholar 

  11. Hanstein, W. G., Davis, K. A., and Hatefi, Y., Archs. Biochem. Biophys., 147, 534 (1971).

    CAS  Article  Google Scholar 

  12. Shih, J.-H. C., and Eiduson, S., Nature, 224, 1309 (1969).

    CAS  Article  Google Scholar 

  13. Youdim, M. B. H., Collins, G. G. S., Sandler, M., Bevan Jones, A. B., Pare, C. M., and Nicholson, W. J., Nature, 236, 225 (1972).

    CAS  Article  Google Scholar 

  14. Eiduson, S., Adv. Biochem. Psychopharmac., 5, 271 (1972).

    CAS  Google Scholar 

  15. Nagatsu, T., Nakano, G., Mizutani, K., and Harada, M., Adv. Biochem. Psychopharmac., 5, 25 (1972).

    CAS  Google Scholar 

  16. Oreland, L., Archs. Biochem. Biophys., 146, 410 (1971).

    CAS  Article  Google Scholar 

  17. Gomes, B., Igaue, I., Kloepfer, H. G., and Yasunobu, K. T., Archs. Biochem. Biophys., 132, 16 (1969).

    CAS  Article  Google Scholar 

  18. Jarrott, B., J. Neurochem., 18, 7 (1971).

    CAS  Article  Google Scholar 

  19. Kroon, M. C., and Veldstra, H., FEBS Lett., 24, 173 (1972).

    CAS  Article  Google Scholar 

  20. Neff, N. H., in Frontiers in Catecholamine Research (edit, by Usdin, E., and Snyder, S. H.) (Pergamon Press, London and New York) (in the press).

  21. Youdim, M. B. H., Trans. Biochem. Soc. (in the press).

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TIPTON, K., HOUSLAY, M. & GARRETT, N. AUotopic Properties of Human Brain Monoamine Oxidase. Nature New Biology 246, 213–214 (1973). https://doi.org/10.1038/newbio246213a0

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