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Some observations on the possible nutritional significance of vitamin B12- and folate-binding proteins in milk

Published online by Cambridge University Press:  07 January 2011

J. E. Ford
J. E. Ford
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading Rg2 9AT
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Abstract

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1. The folate and vitamin B12 in milk are strongly bound to minor whey proteins. These binder proteins are present in excess, and so milk has capacity – which varies between milks of different mammalian species – to sequester added cyanocobalamin and folic acid.

2. A study was made of the influence of different milks on uptake of [3H]cyanocobalamin and [3H]folic acid in selected bacteria, mostly of types that are commonly found in the intestine.

3. None of the test cultures required exogenous vitamin B12. Nevertheless, when free cyanocobalamin was added, in seven of nine cultures it was rapidly taken up into the cells, though there were large differences between the different bacterial species in their absorptive capacity. In presence of sow's milk, little or none of the added cyanocobalamin was taken up, even after incubation of the test mixture for 1 h at 37°. The avidity of sow's milk for cyanocobalamin, as judged from its retention of the vitamin against competition by bacterial cells, was greater than that of a preparation of porcine Intrinsic Factor of similar binding capacity.

4. Of ten cultures of bacteria representing seven species, only the five cultures that required exogenous folate took up added folic acid into the cells. Uptake was severely depressed by the simultaneous addition of goat's colostrum, even after incubation of the test mixture for 1 h at 37°.

5. The physiological role of the binders is discussed. It is postulated that they may act in the mammary gland as trapping mechanisms to accumulate the vitamins from blood plasma into milk and in the gut to facilitate their absorption, both directly, and indirectly by preventing their uptake by intestinal micro-organisms. It is concluded that the binders might well influence the vitamin economy in the neonatal period, and the ecology of the gut microflora.

Type
General Nutrition
Information
British Journal of Nutrition , Volume 31 , Issue 2 , March 1974 , pp. 243 - 257
Copyright
Copyright © The Nutrition Society 1974

References

REFERENCES

Ardeman, S., Chanarin, I. & Berry, V. (1965). Br. J. Haemat. 11, 11.CrossRefGoogle Scholar
Baker, S. J., Kumar, S. & Swaminathan, S. P. (1965). Lancet i, 685.CrossRefGoogle Scholar
Boass, A. & Wilson, T. H. (1963). Am. J. Physiol. 204, 101.Google Scholar
Brambell, F. W. R. (1970). The Transmission of Passive Immunity from Mother to Young p. 269. Amsterdam: North-Holland Publishing Co.Google Scholar
Braude, R., Coates, M. E., Henry, K. M., Kon, S. K., Rowland, S. J., Thompson, S. Y. & Walker, D. M. (1947). Br. J. Nutr. 1, 64.Google Scholar
Bullen, J. J., Rogers, H. J. & Leigh, L. (1972). Br. med. J. i, 69.CrossRefGoogle Scholar
Bullen, C. L. & Willis, A. T. (1971). Br. med. J. iii, 338.CrossRefGoogle Scholar
Burkholder, P. R. (1951). Science, N. Y. 114, 459.Google Scholar
Davies, P. A. (1971). Br. med. J. iv. 351–354.CrossRefGoogle Scholar
De Man, J. C., Rogosa, M. & Sharpe, M. E. (1960). J. appl. Bact. 23, 130.CrossRefGoogle Scholar
Fernell, W. R. & Rosen, G. D. (1956). Br. J. Nutr. 10, 143.Google Scholar
Ford, J. E. (1958). J. gen. Microbiol. 19, 161.CrossRefGoogle Scholar
Ford, J. E. (1962). Br. J. Nutr. 16, 409.CrossRefGoogle Scholar
Ford, J. E. & Goulden, J. D. S. (1959). J. gen. Microbiol. 20, 267.Google Scholar
Ford, J. E., Knaggs, G. S., Salter, D. N. & Scott, K. J. (1972). Br. J. Nutr. 27, 571.Google Scholar
Ford, J. E. & Rogosa, M. (1961). J. gen. Microbiol. 25, 249.Google Scholar
Ford, J. E., Salter, D. N. & Scott, K. J. (1969). J. Dairy Res. 36, 435.CrossRefGoogle Scholar
Giannella, R. A., Broitman, S. A. & Zamcheck, N. (1971). J. clin. Invest. 50, 1100.Google Scholar
Giannella, R. A., Broitman, S. A. & Zamcheck, N. (1972). Gastroenterology 62, 255.CrossRefGoogle Scholar
Glass, G. B. J. (1963). Physiol. Rev. 43, 529.CrossRefGoogle Scholar
Gottlieb, C., Lau, K., Wasserman, L. R. & Herbert, V. (1965). Blood 25, 875.CrossRefGoogle Scholar
Gräsbeck, R., Nyberg, W. & Reizenstein, P. (1958). Proc. Soc. exp. Biol. Med. 97, 780.CrossRefGoogle Scholar
Gregory, M. E. (1954). Br. J. Nutr. 8, 340.Google Scholar
Gregory, M. E., Ford, J. E. & Kon, S. K. (1952). Biochem. J. 51, proc. xxix.Google Scholar
Gregory, M. E. & Holdsworth, E. S. (1955). Biochem. J. 59, 329.Google Scholar
Herbert, V. (1962). Archs intern. Med. 110, 649.CrossRefGoogle Scholar
Hoff-Jorgensen, E. (1952). Archs Biochem. 36, 235.Google Scholar
Izak, G., Galewski, K., Rachmilewitz, M. & Grossowicz, N. (1972). Proc. Soc. exp. Biol. Med. 140, 248.Google Scholar
Klipstein, F. A. & Lipton, S. D. (1970). Am. J. clin. Nutr. 23, 132.CrossRefGoogle Scholar
Matoth, Y., Pinkas, A. & Sroka, C. (1965). Am. J. clin. Nutr. 16, 356.CrossRefGoogle Scholar
Sharpe, M. E. (1964). J. gen. Microbiol. 36, 151.CrossRefGoogle Scholar
Skeggs, H. G., Nepple, H. M., Valentik, K. A., Huff, J. W. & Wright, L. D. (1950). J. biol. Chem. 184, 211.Google Scholar
Ternberg, J. L. & Eakin, R. E. (1949). J. Am. chem. Soc. 71, 3858.Google Scholar
Williams, D. L. & Spray, G. H. (1968). Br. J. Nutr. 22, 297.Google Scholar