Abstract
Oxidative deamination of biogenic monoamines is believed to be accomplished by at least two principal functionally different forms of monoamine oxidase (MAO, EC 1.4.3.4) (Tipton, et al., 1976). In rat brain, serotonin is deaminated by MAO-A whereas phenylethyl amine is deaminated by MAO-B (Jain, 1977). The multiple MAO enzymes which have been localized in the outer mitochondrial membrane are intrinsic membrane-bound flavoproteins (Greenawalt and Schnaitman, 1970). Vigorous procedures involving sonication, organic solvent extraction, and/or detergent treatment are required to solubilize the enzyme with concomitant preferential loss of the MAO-A characteristics (Tipton, 1975). Treatment of the solubilized MAO active fractions with chaotropic agents to remove the lipid moiety results in the disappearance of the apparent multiplicity both in terms of electrophoretic mobility and substrate-inhibitor specificity (Houslay and Tipton, 1973). These results favor the model that the MAO-A and B activities reside with the same enzymic protein. However, immunochemical studies (Dennick and Mayer, 1977; McCauley and Racker, 1973) show equivocal results.
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References
Cawthon, R.M. and Breakefield, X.O. (1979). Differences in A and B forms of monoamine oxidase revealed by limited proteolysis and peptide mapping. Nature 281, 692–694.
Dennick, R.G. and Mayer, R.J. (1977). Purification and immunochemical characterization of monoamine oxidase from rat and human liver. Biochem. J. 161, 167–174.
Greenawalt, J.W. and Schnaitman, C. (1970). An appraisal of the use of monoamine oxidase as an enzyme marker for the outer membrane of rat liver mitochondria. J. Cell. Biol. 46, 173–179.
Houslay, M.D. and Tipton, K.F. (1973). The nature of the electrophoretically separable multiple forms of rat liver monoamine oxidase. Biochem. J. 135, 173–186.
Huang, R.H. and Eiduson, S. (1977). Significance of multiple forms of brain monoamine oxidase in situ as probed by electron spin resonance. J. Biol. Chem. 256, 284–290.
Huang, R.H. (1980). Lipid protein interactions in the multiple forms of monoamine oxidase. Enzymic and ESR studies with purified rat brain mitochondria. Mol. Pharmacol. 17, 192–198.
Huang, R.H. and Faulkner, R. (1980). Lipid-protein interactions in the multiple forms of monoamine oxidases: lipases as probes using purified intact rat brain mitochondria. Mol. Pharmacol. 18, 267–273.
Huang, R.H. (1981). Lipid-protein interactions in the multiple forms of monoamine oxidases: effect of reconstitution. Manuscript in preparation.
Jain, M (1977). Monoamine oxidase. Examination of multiple forms. Life Sci. 20, 1925–1933.
McCauley, R. and Racker, E. (1973). Separation of two monoamine oxidases from bovine brain. Molec. Cell Biochem. 1, 73–81.
Severina, I.S. (1973). On the substrate-binding sites of the active centre of mitochondrial monoamine oxidase. Eur. J. Biochem. 38, 239–246.
Tipton, K.F., Houslay, M.D. and Mantle, T.J. (1976). In Monoamine Oxidase and Its Inhibition. Ciba Foundation Symposium 39, Elsevier, Amsterdam, pp. 5–31.
Tipton, K.F. (1975). Monoamine Oxidase. Am. Physiol. Soc. Handb. Physiol. 6, 677–697.
White, H.L. and Glassman, A.T. (1977). Multiple binding sites of human brain and liver monoamine oxidase: substrate specificities, selective inhibitions and attempts to separate enzyme forms. J. Neurochem. 29, 987–997.
White, L. and Wu, J.C. (1975). Multiple binding sites of human brain monoamine oxidase as indicated by substrate competition. J. Neurochem. 25, 21–26.
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Huang, R.H. (1981). Topology and lipid protein association of MAO-A and MAO-B. In: Usdin, E., Weiner, N., Youdim, M.B.H. (eds) Function and Regulation of Monoamine Enzymes: Basic and Clinical Aspects. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06276-8_54
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DOI: https://doi.org/10.1007/978-1-349-06276-8_54
Publisher Name: Palgrave Macmillan, London
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