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The Effects of Ethanol on Tryptophan Pyrrolase Activity and Their Comparison with Those of Phenobarbitone and Morphine

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Alcohol Intoxication and Withdrawal

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 59))

Abstract

Tryptophan pyrrolase (L-tryptophan-O2 oxidoreductase EC 1.13.11.11) is the first and rate-limiting haem-dependent enzyme of the hepatic kynurenine-nicotinic acid pathway of tryptophan degradation. The importance of this pathway to general body metabolism is evident from the fact that its end-products are the important redox cofactors NAD+ and NADP+. It is also important to the brain because, being the quantitatively most important of all the tryptophan metabolic pathways, its activity can determine the extent of the brain uptake of the amino acid precursor of 5-hydroxytryptamine (5-HT or serotonin), and there is evidence of an inverse relation between liver tryptophan pyrrolase activity and brain 5-HT concentration (Curzon, 1969). The role of 5-HT in the regulation of mood (Curzon, 1969; Lapin Oxenkrug, 1969), and its implication in the actions of alcohol have been previously discussed (Badawy Evans, 1973b).

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References

  • Badawy, A. A.-B. Evans, M. (1972) Lancet, ii, 374–375

    Google Scholar 

  • Badawy, A. A.-B. Evans, M. (1973a) Biochem. Soc. Trans. 1, 193–195

    Google Scholar 

  • Badawy, A. A.-B. Evans, M. (1973b) Advan. Exp. Med. Biol. 35, 105–123

    Article  Google Scholar 

  • Badawy, A. A.-B. Evans, M. (1973c) Biochem. J. 133, 585–591

    Google Scholar 

  • Badawy, A. A.-B. Evans, M. (1973d) Biochem. J. 135, 555–557

    Google Scholar 

  • Badawy, A. A.-B. Evans, M. (1973e) Biochem. J. 136, 885–892

    Google Scholar 

  • Badawy, A. A.-B. Evans, M. (1974) Biochem. J. 138, 445–451

    Google Scholar 

  • Badawy, A. A.-B. Smith, M. J. H. (1971) Biochem. J. 123, 171–174

    Google Scholar 

  • Badawy, A. A.-B. Smith, M. J. H. (1972) Biochem.Pharmacol. 21, 97–101

    Article  Google Scholar 

  • Brodie, B. B., Butler, W. M. Jr., Horning, M. G., Maickel, R. P. Maling, H. M. (1961) Amer. J. Clin. Nutr. 9, 432–435

    Google Scholar 

  • Butcher, R. G. (1971) Biochem. J. 125, 22P - 23 P

    Google Scholar 

  • Butcher, R. W., Robison, G. A., Hardman, J. G. Sutherland, E. W. (1968) Advan. Enz. Regul. 6, 357–389

    Article  Google Scholar 

  • Cho-chung, Y. S. Pitot, H. C. (1967) J. Biol. Chem. 242, 1192–1198

    Google Scholar 

  • Curzon, G. (1969) Brit. J. Psychiat. 115, 1367–1374

    Article  Google Scholar 

  • Curzon, G., Friedel, J. Knott, P. J. (1973) Nature New Biol. 242, 198–200

    Article  Google Scholar 

  • Curzon, G. Knott, P. J. (1974) Brit. J. Pharmacol. 50, 197–204

    Article  Google Scholar 

  • De Matteis, F. (1972) Biochem. J. 130, 52P - 53 P

    Google Scholar 

  • Denkla, W. D. Dewey, H. K. (1967) J. Lab. Clin. Med. 69, 160–169

    Google Scholar 

  • Druyan, R. Kelly, A. (1972) Biochem. J. 129, 1095–1099

    Google Scholar 

  • Ellis, S., Anderson, H. L., Jr. Collins, M. (1953) Proc. Soc. Exp. Biol. Med. 84, 383–386

    Article  Google Scholar 

  • Feigelson, P. Greengard, 0. (1961) J. Biol. Chem. 236, 153–157

    Google Scholar 

  • Greengard, 0. Feigelson, P. (1961) J. Biol. Chem. 236, 158–161

    Google Scholar 

  • Kalant, H., Khanna, J. M. Loth, J. (1970) Can. J. Physiol. Pharmacol. 48, 542–549

    Article  Google Scholar 

  • Katz, J. Wals, P. A. (1970) J. Biol. Chem. 245, 2546–2548

    Google Scholar 

  • Lapin, I. P. Oxenkrug, G. F. (1969) Lancet, i, 132–136

    Google Scholar 

  • Lester, D., Keokosky, W. Z. Felzenberg, F. (1968) Q. J. Stud.Alochol, 29, 449–454

    Google Scholar 

  • Madras, B. K. Sourkes, T. L. (1968) Biochem. Pharmacol. 17, 1037 1047

    Google Scholar 

  • McArthur, J. N. Dawkins, P. D. (1969) J. Pharm. Pharmacol. 21, 744750

    Google Scholar 

  • McIntosh, D. A. D. Topham, J. C. (1972) Biochem. Pharmacol. 21, 1025–1029

    Article  Google Scholar 

  • Mikac-Devic, D.,Stankovic, H. Boskovic, K. (1973) Clin. Chim. Acta, 45, 55–59

    Article  Google Scholar 

  • MvSrland, J. (1974) Biochem. Pharmacol. 23, 21–35

    Article  Google Scholar 

  • MOrland, J., Christoffersen, T., Osnes, J. B., Seglen, P. 0. Jervell, K. F. (1972) Biochem. Pharmacol. 21, 1849–1859

    Article  Google Scholar 

  • Robison, G. A., Butcher, R. W. Sutherland, E. W. (1967) Ann. N. Y. Acad. Sci. 139, 703–723

    Article  Google Scholar 

  • Sardesai, V. M. Provido, H. S. (1972) Life Sci. 11, 1023–1028

    Article  Google Scholar 

  • Satyanarayana Rao, M. R., Malathi, K. Padmanaban, G. (1972) Biochem. J. 127, 553–559

    Google Scholar 

  • Schimke, R.T. (1969) Curr. Top. Cell. Regul. 1, 77–124

    Google Scholar 

  • Seifert, J. (1973) Toxicology, 1, 179–186

    Article  Google Scholar 

  • Shanley, B. C., Zail, S. S. Joubert, S. M. (1968) Lancet, i, 70–71

    Google Scholar 

  • Slater, T. F. (1972) in Free Radical Mechanisms in Tissue Injury (Lagnado, J. R., ed.) pp. 171–197, Pion Ltd., London

    Google Scholar 

  • Slater, T. F. Sawyer, B. (1962) Nature (Lend.) 193, 454–456

    Article  Google Scholar 

  • Slater, T. F., Sawyer, B. Straüli, U. (1964) Arch. Internat. Physiol. Biochim. 72, 427–447

    Google Scholar 

  • Smith, H. G. Lakatos, C. (1971) J. Pharm. Pharmacol. 23, 180–189

    Article  Google Scholar 

  • Tyrrell, D. L. J. Marks, G. S. (1972) Biochem. Pharmacol. 21, 2077–2093

    Article  Google Scholar 

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Authors and Affiliations

  1. Addiction Unit Research Laboratory, Whitchurch Hospital, University Hospital of Wales, Cardiff, CF4 7XB, UK

    A. A.-B. Badawy & M. Evans

Authors
  1. A. A.-B. Badawy
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  2. M. Evans
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Editors and Affiliations

  1. Downstate Medical Center, Brooklyn, New York, USA

    Milton M. Gross (Chairman) (Chairman)

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Badawy, A.AB., Evans, M. (1975). The Effects of Ethanol on Tryptophan Pyrrolase Activity and Their Comparison with Those of Phenobarbitone and Morphine. In: Gross, M.M. (eds) Alcohol Intoxication and Withdrawal. Advances in Experimental Medicine and Biology, vol 59. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-0632-1_15

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  • DOI: https://doi.org/10.1007/978-1-4757-0632-1_15

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-0634-5

  • Online ISBN: 978-1-4757-0632-1

  • eBook Packages: Springer Book Archive

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