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The Course of Microbial Infection of the Hen's Egg

1966; Wiley; Volume: 29; Issue: 2 Linguagem: Inglês

10.1111/j.1365-2672.1966.tb03482.x

2056-5232

R. G. Board,

Bacterial Genetics and Biotechnology

Journal of Applied BacteriologyVolume 29, Issue 2 p. 319-341 Free Access The Course of Microbial Infection of the Hen's Egg R. G. BOARD, R. G. BOARD School of Biological Sciences, University of Bath, Claverton Down, Bath, EnglandSearch for more papers by this author R. G. BOARD, R. G. BOARD School of Biological Sciences, University of Bath, Claverton Down, Bath, EnglandSearch for more papers by this author First published: August 1966 https://doi.org/10.1111/j.1365-2672.1966.tb03482.xCitations: 87AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat 6. References Alford, L. R., Holmes, N. E., Scott, W. J. & Vickery, J. R. (1950). Studies in the preservation of shell eggs. 1. Nature of wastage in Australian export eggs. Aust. J. appl. Sci. 1, 208. Google Scholar Alderton, G., Ward, W. H. & Fevold, H. L. (1946). Identification of the bacteria-inhibiting, iron-binding protein of egg white as conalbumin. Archs Biochem. 11, 9. CASPubMedWeb of Science®Google Scholar Ayres, J. C. (1958). Methods for depleting glucose from egg albumen before drying. Fd Technol., Champaign 12, 186. CASWeb of Science®Google Scholar Ayres, J. C. & Taylor, B. (1956). Effect of temperature on microbial proliferation in shell eggs. Appl. Microbiol. 4, 355. CASPubMedWeb of Science®Google Scholar Azari, P. R. & Feeney, R. E. (1958). Resistance of metal complexes of conalbumin and transferrin to proteolysis and to thermal denaturation. J. biol. Chem. 232, 293. 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