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Zinc transport proteins in plasma

Published online by Cambridge University Press:  09 March 2007

J. K. Chesters
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
Marie Will
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
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Abstract

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1. Both albumin and transferrin have been suggested as carriers of zinc in plasma. Their relative importance in Zn transport was therefore investigated as a preliminary to a study of the rates of passage of Zn through plasma.

2. The apparent log stability constant for Zn binding to human apotransferrin at pH 7·4 was estimated to be approximately 5·9 which is substantially lower than previous reports of 7·0 for the corresponding value for Zn binding to albumin (Giroux & Henkin, 1972).

3. When the relative abilities of human albumin and apotransferrin to compete for Zn with low-molecular-weight chelators were compared at the same relative concentrations of these proteins as are found in plasma, albumin retained substantially more Zn than transferrin.

4. It seems likely that albumin acts as the major transport protein for Zn in plasma of most species, Zn also being present firmly bound to α2-macroglobulin.

5. In porcine plasma or serum however, there were three major Zn-binding proteins, two of which were probably albumin and α2-macroglobulin. The nature of the third component remains unknown but it appeared to have a molecular weight of between 100000–140000, it was precipitated by 2·2 M-ammonium sulphate and by 150 gpolyethylene glycol/l.

6. There were no significant differences in Zn distribution in plasma of porcine blood obtained from the aorta, the posterior vena cava or from the hepatic portal vein but use of heparin as an anticoagulant altered the normal pattern of distribution of Zn in plasma.

Type
Papers on General Nutrition
Copyright
Copyright © The Nutrition Society 1981

References

REFERENCES

Bolton, A. E. (1977). Radioiodination Techniques. Amersham, England: Radiochemical Centre.Google Scholar
Boyett, J. D. & Sullivan, J. F. (1970). Metabolism 19, 148.CrossRefGoogle Scholar
Charlwood, P. A. (1979). Biochim. biophys. Acta 581, 260.CrossRefGoogle Scholar
Chesters, J. K. & Will, M. (1978). Br. J. Nutr. 39, 297.CrossRefGoogle Scholar
Chesters, J. K. & Will, M. (1981). Br. J. Nutr. 46, 119.CrossRefGoogle Scholar
Corrigall, W., Dalgarno, A. C., Ewen, L. A. & Williams, R. B. (1976). Vet. Rec. 99, 396.CrossRefGoogle Scholar
Evans, G. (1976). Proc. Soc. exp. Biol. Med. 151, 775.CrossRefGoogle Scholar
Evans, G. & Winter, T. W. (1975). Biochem. biophys. Res. Commun. 66, 1218.CrossRefGoogle Scholar
Giroux, E. L. (1975). Biochem. Med. 12, 258.CrossRefGoogle Scholar
Giroux, E. I. & Henkin, R. I. (1972). Biochim. biophys. Acta 273, 64.CrossRefGoogle Scholar
Hallbook, T. & Hedelin, H. (1977). Br. J. Surg. 64, 271.CrossRefGoogle Scholar
Hannig, K. (1961). Z. analyt. Chem. 181, 244.CrossRefGoogle Scholar
Himmelhoch, S. R., Sober, H. A., Vallee, B. L., Peterson, E. A. & Fuwa, K. (1966). Biochemistry, N. Y. 5, 2523.CrossRefGoogle Scholar
Mann, K. G., Fish, W. W., Cox, A. C. & Tanford, C. (1970). Biochemistry, N. Y. 9, 1348.CrossRefGoogle Scholar
Nagy, B. & Lehrer, S. S. (1972). Archs Biochem. Biophys. 148, 27.CrossRefGoogle Scholar
Nandedkar, A. K. N., Hong, M. S. & Friedberg, F. (1974). Biochem. Med. 9, 177.CrossRefGoogle Scholar
Parisi, A. F. & Vallee, B. L. (1970). Biochemistry, N. Y. 9, 2421.CrossRefGoogle Scholar
Pekarek, R. S. & Beisel, W. R. (1969). Appl. Microbiol. 18, 482.CrossRefGoogle Scholar
Scott, D. & McIntosh, G. H. (1975). Q. Jl. exp. Physiol. 60, 131.CrossRefGoogle Scholar
Sillen, L. G. & Martell, A. E. (1964). Spec. Publs chem. Soc. 17.Google Scholar
Sillen, L. G. & Martell, A. E. (1971). Spec. Publs chem. Soc. 25.Google Scholar
Smith, K. T., Failla, M. L. & Cousins, R. J. (1978). Biochem. J. 184, 627.CrossRefGoogle Scholar
Tan, A. T. & Woodworth, R. C. (1969). Biochemistry, N. Y. 8, 3711.CrossRefGoogle Scholar
Vikbladh, I. (1951). Scand. J. clin. Lab. Invest. 3, Suppl. 2.Google Scholar
Whitenack, D. L., Whitehair, C. K. & Miller, E. R. (1978). Am. J. vet. Res. 39, 1447.Google Scholar