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The Active Site of Plasma Amine Oxidase “The Key Enzyme of Biogenic Amines Degradation in Plasma” as Seen by Fluorescence Investigations

  • Henry M. Zeidan
  • S. Oyouga
Part of the Biodeterioration Research book series (BIOR, volume 4)

Abstract

The role of Plasma Amine Oxidase (diamino: O2 oxidoreductase; EC 1.4.3.6) in the catabolism of various amines found in association with DNA and its function in one of the catabolic pathways of histamine and other pharmacologically important amines have led to considerable interest in this enzyme. The enzyme catalyzes the oxidation of certain amines and diamines according to the following reaction:
$$RC{H_2}N{H_2} + {O_2} + {H_2}O - - - - - RCHO + N{H_3} + {H_2}{O_2}$$
Physicochemical studies of bovine plasma amine oxidase indicated that the enzyme is made up of two identical subunits and has a molecular weight of 170,000 KD (Yasunobu et al., 1976). The enzyme contains one essential histidine residue per monomer (Hiramatsu, et al., 1975). There are two gram-atom Cu/ mole protein which are essential for enzyme activity (Yasunobu et al., 1976). It has been reported that the copper does not change its valence state during catalysis either under aerobic or anaerobic addition of substrate. The only variance to the no valence change was the work reported by Mondovi et al., 1976 who reported that copper changed its valence state during substrate oxidation. It was concluded acid analysis was performed on the native enzyme and the reduced modified enzyme. The concentration of the protein was determined by a biuret method and absorbance was read at 280nm (R = 13). N-(1-pyrene) maleimide was purchased from Molecular Probes. The other common reagents used were of reagent grade and were purchased from standard companies.

Keywords

Emission Spectrum Fluorescence Spectrum Sulfhydryl Group Amine Oxidase Pyridoxal Phosphate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Achee, F.M., Chervenka, C.H., Smith, R.A. and Yasunobu, K. (1968), Biochemistry, 128, 7, 4329–4335.CrossRefGoogle Scholar
  2. Davidson, A.N. (1958) Phvsiol. Rev., 38, 729–747.Google Scholar
  3. Hiramatsu, A., Tsurushin, S., and Yasunobu, K.T. (1975), Eur. J. Biol. Chem., 57, 587–593.CrossRefGoogle Scholar
  4. Inamasu, M., Yasunobu, K.T., and Konig, W.A. (1974), J. Biol. Chem., 249, 5265–5268.Google Scholar
  5. Mondovi, B., Costa, M.T., Argo, A.F., and Rotilo, G., (1976), Arch. Biochem. Biophys., 119, 373–381.CrossRefGoogle Scholar
  6. Suva, R.H., and Abewles, R.H. (1978), Biochemistry, 17, 3538–3546.CrossRefGoogle Scholar
  7. Watanabe, K., Smith, R.A., Inamasu, M., and Yasunobu, K.T. (1972), Adv. Biochem. Psvchodharmacol., 5, 107–117.Google Scholar
  8. Weltman, J.K. (19731., J. Biol. Chem., 248, 3173.Google Scholar
  9. Wu, Cheng-Wen, Yarbough, L. and Wu, F. (1976), Biochem., 15, 2863–2867.CrossRefGoogle Scholar
  10. Yasunobu, K.T., Minamiura, N., and Ishizaki, H. (1976), Mol Cell. Biochem., 13 3–29.CrossRefGoogle Scholar
  11. Zeidan, H., Watanabe, K., Piette, L.H., and Yasunobu, K. (1980), J. Biol. Chem., 255, 7621–7626.Google Scholar
  12. Zeidan, H., and Buchanan, S. (1990), Biodeterioration Research, 3, 565–576, G Llewellyn and C. O’Rear (eds.), Plenum Press, N.Y.Google Scholar

Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Henry M. Zeidan
    • 1
    • 2
    • 3
  • S. Oyouga
    • 1
    • 2
    • 3
  1. 1.Chemistry DepartmentClark Atlanta UniversityAtlantaUSA
  2. 2.Chemistry DepartmentUniversity of TexasEl-PasoUSA
  3. 3.Life CollegeMariettaUSA

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