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The fate of 99Mo-labelled sodium tetrathiomolybdate after duodenal administration in sheep: the effect on caeruloplasmin (EC 1.16.3.1) diamine oxidase activity and plasma copper

Published online by Cambridge University Press:  09 March 2007

J. Mason ,
M. Lamand  and
C. A. Kelleher
J. Mason
Affiliation:
Biochemistry Department, Trinity College, Dirblin 2, Ireland
M. Lamand
Affiliation:
Biochemistry Department, Trinity College, Dirblin 2, Ireland
C. A. Kelleher
Affiliation:
Biochemistry Department, Trinity College, Dirblin 2, Ireland
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Abstract

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1. The effect of acute duodenal infusion of 99Mo-labelled sodium tetrathiomolybdate on caeruloplasmin (ferroxidase; EC 1.16.3.1) was examined in sheep. The diamine oxidase activity of this enzyme with respect to two substrates, p-phenylenediamine and o-dianisidine (both at their apparent Km concentrations) was inhibited.

2. The 99Mo appeared rapidly in plasma and was at first present predominantly in a trichloroacetic acid insoluble form; inhibition of oxidase activity was related to the levels of TCA-insoluble Mo. The behaviour of the copper prosthetic groups of caeruloplasmin was altered since some plasma Cu precipitated with the protein fraction after TCA treatment. The appearance of TCA insoluble Cu was related to the level of TCA-insoluble 99Mo and corresponded to the inhibition of diamine oxidase activity.

Type
Papers on General Nutrition
Information
British Journal of Nutrition , Volume 43 , Issue 3 , May 1980 , pp. 515 - 523
Copyright
Copyright © The Nutrition Society 1980

References

REFERENCES

Agarwal, A. G. (1975). New Sci. 65, 260.Google Scholar
Bremner, I. (1975). Proc. Nutr. Soc. 35, 22A.Google Scholar
Bremner, I. & Young, B. W. (1978). Br. J. Nutr. 39, 325.CrossRefGoogle Scholar
Dick, A. T. (1953). Aust. Vet. J. 29, 18.CrossRefGoogle Scholar
Dick, A. T., Dewey, D. W. & Gawthome, J. M. (1975). J. agric. Sci., Camb. 85, 567.CrossRefGoogle Scholar
El Gallad, T. T., Bremner, 1. P. & Mills, G. F. (1977). Proc. Nutr. Soc. 36, 104A.Google Scholar
Frieden, E. & Hsieh, H. S. (1976). Adv. Enzymol. 44, 187.Google Scholar
Grace, N. D. & Suttle, N. F. (1979). Br. J. Nutr. 41, 125.CrossRefGoogle Scholar
Kelleher, C. A. & Mason, J. (1979). Res. vet. Sci. 26, 124.Google Scholar
Mason, J. (1978). Vet. Sci. Comm. 2, 85.CrossRefGoogle Scholar
Mason, J. & Cardin, C. J. (1977). Res. vet. Sci. 22, 313.CrossRefGoogle Scholar
Mason, J., Cardin, C. J. & Dennehy, A. (1978). Res. vet Sci. 24, 104.CrossRefGoogle Scholar
Mason, J., Lamand, M., Tressol, J. C. & Lab, C. (1978). Ann Rech. Vet. 9, 577.Google Scholar
Mills, C. F., Bremner, I., El Gallad, T. T., Dalgarno, A. C. & Young, B. W. (1978). In Trace Element Metabolism in Man and Animals, p. 150 [Kirchgessner, M., editor]. Weinhenstephan: Arbeitskreis für Tierernahrungsforschung.Google Scholar
Pitt, M. A. (1976). In Agents and Actions, vol. 6, p. 758. Basel: Birkhauser Verlag.Google Scholar
Smith, B. S. W. & Wright, H. (1975). J. Comp. Path. 85, 299.CrossRefGoogle Scholar
Suttle, N. F. (1974). Proc. Nutr. Soc. 33, 299.CrossRefGoogle Scholar
Weber, K. M., Leaver, D. D. & Wedd, A. G. (1979). Br. J. Nurr. 41, 403.Google Scholar