Hostname: page-component-848d4c4894-4rdrl Total loading time: 0 Render date: 2024-06-30T10:40:15.880Z Has data issue: false hasContentIssue false

Riboflavin metabolism of cows and goats and rate of biosynthesis of riboflavin by the lactating goat

Published online by Cambridge University Press:  09 March 2007

Audrey Crossland
Affiliation:
Hannah Dairy Research Institute, Kirkhill, Ayr
E. C. Owen
Affiliation:
Hannah Dairy Research Institute, Kirkhill, Ayr
R. Proudfoot
Affiliation:
Hannah Dairy Research Institute, Kirkhill, Ayr
Rights & Permissions [Opens in a new window]

Abstract

Image of the first page of this content. For PDF version, please use the ‘Save PDF’ preceeding this image.'
Type
Research Article
Copyright
Copyright © The Nutrition Society 1958

References

Axelrod, A. E. & Elvehjem, C. A. (1941). J. biol. Chem. 140, 725.Google Scholar
Barton-Wright, E. C. & Booth, R. G. (1943). Biochem. J. 37, 25.Google Scholar
Bavetta, L. A. & Narrod, S. A. (1957). Proc. Soc. exp. Biol., N. Y., 94, 289.CrossRefGoogle Scholar
Bessey, O. A., Lowry, O. H. & Love, R. H. (1949). J. biol. Chem. 180, 755.CrossRefGoogle Scholar
Corbett, J. L. (1957). N. A. A. S. quart. Rev. 37, 93.Google Scholar
Crammer, J. L. (1948). Nature, Lond., 161, 349.Google Scholar
Crossland, A. C., Owen, E. C. & Proudfoot, R. (1958). Biochem. J. 68, 14P.Google Scholar
De Renzo, E. C. (1956). Advanc. Enzymol. 17, 293.Google Scholar
Edwards, D. C. (1955). J. Dairy Res. 22, 232.CrossRefGoogle Scholar
Edwards, D. C. & Darroch, R. A. (1956). Brit. J. Nutr. 10, 286.CrossRefGoogle Scholar
Ferrebee, J. W. (1940). J. clin. Invest. 19, 251.Google Scholar
Greene, R. D. & Black, A. (1937). J. Amer. chem. Soc. 59, 1820.Google Scholar
Holloway, D. H. (1956). Electrical Times, 18 October.Google Scholar
Hunt, C. H., Kick, C. H., Burroughs, E. W., Bethke, R. M., Schalk, A. F. & Gerlaugh, P. (1941). J. Nutr. 21, 85.CrossRefGoogle Scholar
Johnson, P., Maynard, L. A. & Loosli, J. K. (1941). J. Dairy Sci. 24, 57.CrossRefGoogle Scholar
Kawerau, E. (1951). Biochem. J. 48, 281.CrossRefGoogle Scholar
Kiermeier, F. & Capellari, K. (1957). Naturwissenschaften, 44, 69.CrossRefGoogle Scholar
Koschara, W. (1934). Hoppe-Seyl. Z. 229, 103.CrossRefGoogle Scholar
Koschara, W. (1935). Hoppe-Seyl. Z. 232, 101.CrossRefGoogle Scholar
Lewis, J. R. & Gorham, P. R. (1947). Canadian J. Res. 25, Sect. F, p. 133.CrossRefGoogle Scholar
Lowry, O. H. (1948). J. biol. Chem. 173, 677.CrossRefGoogle Scholar
McElroy, L. W. & Goss, H. (1939). J. biol. Chem. 130, 437.CrossRefGoogle Scholar
Mahler, H. R. (1956). Advanc. Enzymol. 17, 233.Google Scholar
Modi, V. V. & Owen, E. C. (1956). Nature, Lond., 178, 1120.CrossRefGoogle Scholar
Owen, E. C. (1947). J. Dairy Res. 15, 142.CrossRefGoogle Scholar
Owen, E. C. (1951). J. Dairy Res. 18, 113.CrossRefGoogle Scholar
Owen, E. C. (1954). J. Dairy Res. 21, 408.CrossRefGoogle Scholar
Pearson, P. B. & Schweigert, B. S. (1947). J. Nutr. 34, 443.CrossRefGoogle Scholar
Richert, D. A. & Westerfield, W. W. (1957). J. biol. Chem. 227, 533.CrossRefGoogle Scholar
Snell, E. E. & Strong, F. M. (1939 a). Industr. Engng Chem. (Anal.), 11, 346.CrossRefGoogle Scholar
Snell, E. E. & Strong, F. M. (1939 b). Enzymologia, 6, 186.Google Scholar
Westerfield, W. W., Richert, D. A. & Higgins, E. S. (1956). In A Symposium on Inorganic Nitrogen Metabolism. Function of Metalloflavo-Proteins. [McElroy, W. and Glass, B. editors.] Baltimore: The John Hopkins Press.Google Scholar
Whitby, L. G. (19511952). Biochem. J. 50, 433.CrossRefGoogle Scholar
Zittle, C. A., Dellamonica, E. S., Custer, J. H. & Rudd, R. K. (1956). J. Dairy Sci. 39, 522.CrossRefGoogle Scholar